9ovv

Heteromeric GluA1/A2-CNIH1 in the activated state, composite map of LBD-TMD

Method: ELECTRON MICROSCOPY D_max: 154.9 Å Quality: EXCELLENT

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Isoform Flip of Glutamate receptor 1

Rattus norvegicus

UniProt P19490

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 403–833 Chain C； UniProt 403–833	Not recorded	Isoform Flip of Glutamate receptor 2 × 2 （P19491） Protein cornichon homolog 1 × 4 （O95406） GLU GLUTAMIC ACID × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 16 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2 NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8；150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 500 uM (R,R)-2b, 1 mM glutamate cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.76 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 9OVV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3SAJ Crystal Structure of glutamate receptor GluA1 Amino Terminal Domain Deposited 2011-06-02	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 22–392（371 aa） Fragment：N-terminal domain (UNP residues 22-392) Chain C 22–392（371 aa） Fragment：N-terminal domain (UNP residues 22-392)	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5；290 K；22% PEG3350, 0.2 M magnesium chloride, 0.1 M sodium acetate, pH 5.0, EVAPORATION, temperature 290K	Resolution 2.50 Å R-free 0.286
3SAJ Crystal Structure of glutamate receptor GluA1 Amino Terminal Domain Deposited 2011-06-02	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 22–392（371 aa） Fragment：N-terminal domain (UNP residues 22-392) Chain D 22–392（371 aa） Fragment：N-terminal domain (UNP residues 22-392)	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5；290 K；22% PEG3350, 0.2 M magnesium chloride, 0.1 M sodium acetate, pH 5.0, EVAPORATION, temperature 290K	Resolution 2.50 Å R-free 0.286
6NJL Architecture and subunit arrangement of native AMPA receptors Deposited 2019-01-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.70 Å
6NJN Architecture and subunit arrangement of native AMPA receptors Deposited 2019-01-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain A 1–907（907 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.50 Å
6QKC GluA1/2 In complex with auxiliary subunit gamma-8 Deposited 2019-01-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM TRIS, pH 8, 150 mM NaCl and 0.1 % digitonin (w/v) cryo-EM vitrification conditions Cryogen ETHANE；3uL on grid, 60 sec incubation and 4sec blotting time	Resolution 4.40 Å
6QKZ Full length GluA1/2-gamma8 complex Deposited 2019-01-30	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 20–907（888 aa） Chain C 20–907（888 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM TRIS, pH 8, 150 mM NaCl and 0.1 % digitonin (w/v) cryo-EM vitrification conditions Cryogen ETHANE；3uL on grid, 60 sec incubation and 4sec blotting time	Resolution 6.30 Å
7OCA Resting state full-length GluA1/A2 heterotertramer in complex with TARP gamma 8 and CNIH2 Deposited 2021-04-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 46 CLR CHOLESTEROL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7OCC NTD of resting state GluA1/A2 heterotertramer Deposited 2021-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–907（907 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7OCC NTD of resting state GluA1/A2 heterotertramer Deposited 2021-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–907（907 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7OCD Resting state GluA1/A2 heterotetramer in complex with auxiliary subunit TARP gamma 8 (LBD-TMD) Deposited 2021-04-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
7OCE Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and CNIH2 (LBD-TMD) Deposited 2021-04-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 46 CLR CHOLESTEROL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
7OCF Active state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and CNIH2 (LBD-TMD) Deposited 2021-04-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	CYZ CYCLOTHIAZIDE × 4 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 26 GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7QHB Active state of GluA1/2 in complex with TARP gamma 8, L-glutamate and CTZ Deposited 2021-12-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	PAM PALMITOLEIC ACID × 14 GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 79N (2S)-2,3-dihydroxypropyl (7Z)-hexadec-7-enoate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM TRIS 150 mM NaCl 0.02 % GDN 87 uM CTZ 100 mM L-Glu cryo-EM vitrification conditions Cryogen ETHANE；3-4 second blots	Resolution 3.50 Å
7QHH Desensitized state of GluA1/2 AMPA receptor in complex with TARP-gamma 8 (TMD-LBD) Deposited 2021-12-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	GLU GLUTAMIC ACID × 4 PAM PALMITOLEIC ACID × 10 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 79N (2S)-2,3-dihydroxypropyl (7Z)-hexadec-7-enoate × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM TRIS 150 mM NaCl 0.02 % GDN 87 uM CTZ 100 mM L-Glu cryo-EM vitrification conditions Cryogen ETHANE；3-4 second blots	Resolution 3.60 Å
8AYL Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand JNJ-61432059 Deposited 2022-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 PLM PALMITIC ACID × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 OIJ 5-[2-(4-fluorophenyl)-7-(4-oxidanylpiperidin-1-yl)pyrazolo[1,5-c]pyrimidin-3-yl]-1,3-dihydroindol-2-one × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8AYM Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand JNJ-55511118 Deposited 2022-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	XVD 6-[2-chloro-6-(trifluoromethoxy)phenyl]-1H-benzimidazol-2-ol × 2 PLM PALMITIC ACID × 14 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8AYN Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand LY3130481 Deposited 2022-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 PLM PALMITIC ACID × 14 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4 OLR 6-[(1~{S})-1-[1-[5-(2-hydroxyethyloxy)pyridin-2-yl]pyrazol-3-yl]ethyl]-3~{H}-1,3-benzothiazol-2-one × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
8AYO Open state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand JNJ-61432059 Deposited 2022-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–907（907 aa） Chain C 1–907（907 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 PLM PALMITIC ACID × 10 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 2 OIJ 5-[2-(4-fluorophenyl)-7-(4-oxidanylpiperidin-1-yl)pyrazolo[1,5-c]pyrimidin-3-yl]-1,3-dihydroindol-2-one × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8C1P Active state homomeric GluA1 AMPA receptor in complex with TARP gamma 3 Deposited 2022-12-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain B 1–907（907 aa） Chain C 1–907（907 aa） Chain D 1–907（907 aa）	Not recorded	CYZ CYCLOTHIAZIDE × 4 PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 GLU GLUTAMIC ACID × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
8C1Q Resting state homomeric GluA1 AMPA receptor in complex with TARP gamma 3 Deposited 2022-12-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain B 1–907（907 aa） Chain C 1–907（907 aa） Chain D 1–907（907 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PLM PALMITIC ACID × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.82 Å
8C2H Transmembrane domain of active state homomeric GluA1 AMPA receptor in tandem with TARP gamma 3 Deposited 2022-12-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain B 1–907（907 aa） Chain C 1–907（907 aa） Chain D 1–907（907 aa）	Not recorded	PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.64 Å
8C2I Transmembrane domain of resting state homomeric GluA1 AMPA receptor in complex with TARP gamma 3 Deposited 2022-12-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain B 1–907（907 aa） Chain C 1–907（907 aa） Chain D 1–907（907 aa）	Not recorded	PLM PALMITIC ACID × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
8P3T Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 1 Deposited 2023-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain B 1–907（907 aa） Chain C 1–907（907 aa） Chain D 1–907（907 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.39 Å
8P3U Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 2 Deposited 2023-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain B 1–907（907 aa） Chain C 1–907（907 aa） Chain D 1–907（907 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.77 Å
8P3V Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 3 Deposited 2023-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain B 1–907（907 aa） Chain C 1–907（907 aa） Chain D 1–907（907 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.53 Å
8P3W Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 4 Deposited 2023-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–907（907 aa） Chain B 1–907（907 aa） Chain C 1–907（907 aa） Chain D 1–907（907 aa）	Not recorded	PLM PALMITIC ACID × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.53 Å
9NR6 The structure of Noelin 1 with cerebellar GluA1/A4-ATD Deposited 2025-03-14	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain A 19–391（373 aa） Chain C 19–391（373 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.26 Å
9NR7 The structure of GluA1/A4 LBD-TMD in Noelin-AMPAR complex Deposited 2025-03-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 407–833（427 aa） Chain C 407–833（427 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.18 Å
9NR8 The structure of cerebellar GluA1/A4 ATD Deposited 2025-03-14	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 19–391（373 aa） Chain C 19–391（373 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.53 Å
9NR9 The structure of GluA1/A4 LBD-TMD with 2 TARPs Deposited 2025-03-14	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 407–833（427 aa） Chain C 407–833（427 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.22 Å
9NRA The structure of GluA1/A4 LBD-TMD with 4 auxiliary subunits Deposited 2025-03-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 407–833（427 aa） Chain C 407–833（427 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.18 Å
9OVT Heteromeric GluA1/A2 in the inactive state, composite map of LBD-TMD Deposited 2025-05-31	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 403–833（431 aa） Chain C 403–833（431 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NA SODIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8；150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 100 uM ZK-200775 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.43 Å
9OVU Composite map of GluA1/A2 in the activated state, in complex with positive allosteric modulator (R,R)-2b and agonist glutamate (ATD-LBD-TMD) Deposited 2025-05-31	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–841（841 aa） Chain C 1–841（841 aa）	Not recorded	GLU GLUTAMIC ACID × 4 NA SODIUM ION × 1 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 500 uM (R,R)-2b, 1 mM glutamate cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9OVW Heteromeric GluA1/A2 in the desensitized state, composite map of ATD-LBD-TMD Deposited 2025-05-31	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 23–833（811 aa） Chain C 23–833（811 aa）	Not recorded	QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 1 mM quiqualate cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.91 Å

32 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GRIA1_RAT
Isoform	P19490-2
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–431； UniProt 403–833 Author chain C； PDBConstruct 1–431； UniProt 403–833

Isoform Flip of Glutamate receptor 2

Rattus norvegicus

UniProt P19491

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain B； UniProt 413–840 Chain D； UniProt 413–840	Not recorded	Isoform Flip of Glutamate receptor 1 × 2 （P19490） Protein cornichon homolog 1 × 4 （O95406） GLU GLUTAMIC ACID × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 16 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2 NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8；150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 500 uM (R,R)-2b, 1 mM glutamate cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.76 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9OVV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1FTJ CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH GLUTAMATE AT 1.9 RESOLUTION Deposited 2000-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J))	Not recorded	ZN ZINC ION × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M Cacodylate 15% PEG 8000 0.2 M Zinc Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 4K	Resolution 1.90 Å R-free 0.266
1FTJ CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH GLUTAMATE AT 1.9 RESOLUTION Deposited 2000-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J))	Not recorded	ZN ZINC ION × 2 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M Cacodylate 15% PEG 8000 0.2 M Zinc Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 4K	Resolution 1.90 Å R-free 0.266
1FTJ CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH GLUTAMATE AT 1.9 RESOLUTION Deposited 2000-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J))	Not recorded	ZN ZINC ION × 2 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M Cacodylate 15% PEG 8000 0.2 M Zinc Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 4K	Resolution 1.90 Å R-free 0.266
1FTJ CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH GLUTAMATE AT 1.9 RESOLUTION Deposited 2000-09-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J))	Not recorded	ZN ZINC ION × 5 GLU GLUTAMIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M Cacodylate 15% PEG 8000 0.2 M Zinc Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 4K	Resolution 1.90 Å R-free 0.266
1FTJ CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH GLUTAMATE AT 1.9 RESOLUTION Deposited 2000-09-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J)) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J))	Not recorded	ZN ZINC ION × 3 GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M Cacodylate 15% PEG 8000 0.2 M Zinc Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 4K	Resolution 1.90 Å R-free 0.266
1FTK CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2I) IN COMPLEX WITH KAINATE AT 1.6 A RESOLUTION Deposited 2000-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 404–528（125 aa） Fragment：LIGAND BINDING CORE, S1S2I Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE, S1S2I	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15% PEG 8000 50 mM potassium phosphate , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.60 Å R-free 0.261
1FTL CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH THE ANTAGONIST DNQX AT 1.8 A RESOLUTION Deposited 2000-09-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	DNQ 6,7-DINITROQUINOXALINE-2,3-DIONE × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；19% PEG 4000 0.3 M ammonium sulfate 0.1 M sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.272
1FTM CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH AMPA AT 1.7 RESOLUTION Deposited 2000-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 1 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15% PEG 8000 0.2 M Zinc Acetate 0.1 M Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.247
1FTM CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH AMPA AT 1.7 RESOLUTION Deposited 2000-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 2 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15% PEG 8000 0.2 M Zinc Acetate 0.1 M Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.247
1FTM CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH AMPA AT 1.7 RESOLUTION Deposited 2000-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 413–527（115 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 2 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15% PEG 8000 0.2 M Zinc Acetate 0.1 M Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.247
1FTM CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH AMPA AT 1.7 RESOLUTION Deposited 2000-09-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15% PEG 8000 0.2 M Zinc Acetate 0.1 M Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.247
1FTM CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH AMPA AT 1.7 RESOLUTION Deposited 2000-09-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：GLUR2-FLOP LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15% PEG 8000 0.2 M Zinc Acetate 0.1 M Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.247
1FTO CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE AT 2.0 A RESOLUTION Deposited 2000-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；22% PEG 8000 0.3 M ammonium sulfate 0.1 M sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.287
1FTO CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE AT 2.0 A RESOLUTION Deposited 2000-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；22% PEG 8000 0.3 M ammonium sulfate 0.1 M sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.287
1FW0 CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH KAINATE AT 2.0 A RESOLUTION Deposited 2000-09-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；274 K；10% PEG 1450, 0.1 M sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 274K	Resolution 1.90 Å R-free 0.308
1GR2 STRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (GLUR2) COMPLEXED WITH KAINATE Deposited 1998-09-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 404–528（125 aa） Fragment：LIGAND BINDING DOMAIN Chain A 652–796（145 aa） Fragment：LIGAND BINDING DOMAIN	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；50 MM KIPI, PH 5.0, 14% PEG 8K	Resolution 1.90 Å R-free 0.273
1LB8 Crystal structure of the Non-desensitizing GluR2 ligand binding core mutant (S1S2J-L483Y) in complex with AMPA at 2.3 resolution Deposited 2002-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：ligand-binding core (flop) Chain A 653–796（144 aa） Fragment：ligand-binding core (flop)	Mutation：L483Y Mutation：L483Y	AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；PEG 8000, ammonium sulfate, sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.30 Å R-free 0.267
1LB8 Crystal structure of the Non-desensitizing GluR2 ligand binding core mutant (S1S2J-L483Y) in complex with AMPA at 2.3 resolution Deposited 2002-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：ligand-binding core (flop) Chain B 653–796（144 aa） Fragment：ligand-binding core (flop)	Mutation：L483Y Mutation：L483Y	AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；PEG 8000, ammonium sulfate, sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.30 Å R-free 0.267
1LB9 Crystal structure of the Non-desensitizing GluR2 ligand binding core mutant (S1S2J-L483Y) in complex with antagonist DNQX at 2.3 A resolution Deposited 2002-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：ligand binding core (flop) Chain A 653–796（144 aa） Fragment：ligand binding core (flop)	Mutation：L483Y Mutation：L483Y	DNQ 6,7-DINITROQUINOXALINE-2,3-DIONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；PEG 4000, ammonium sulfate, sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.30 Å R-free 0.268
1LB9 Crystal structure of the Non-desensitizing GluR2 ligand binding core mutant (S1S2J-L483Y) in complex with antagonist DNQX at 2.3 A resolution Deposited 2002-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：ligand binding core (flop) Chain B 653–796（144 aa） Fragment：ligand binding core (flop)	Mutation：L483Y Mutation：L483Y	DNQ 6,7-DINITROQUINOXALINE-2,3-DIONE × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；PEG 4000, ammonium sulfate, sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.30 Å R-free 0.268
1LBB Crystal structure of the GluR2 ligand binding domain mutant (S1S2J-N754D) in complex with kainate at 2.1 A resolution Deposited 2002-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：ligand binding core (flop) Chain A 653–796（144 aa） Fragment：ligand binding core (flop)	Mutation：N754D Mutation：N754D	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 1000, Li2SO4, phosphate-citrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.10 Å R-free 0.260
1M5B X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH 2-Me-Tet-AMPA AT 1.85 A RESOLUTION. Deposited 2002-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：flop ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：flop ligand binding core (S1S2J) Chain C 413–527（115 aa） Fragment：flop ligand binding core (S1S2J) Chain C 653–796（144 aa） Fragment：flop ligand binding core (S1S2J)	Not recorded	ZN ZINC ION × 3 BN1 (S)-2-AMINO-3-[3-HYDROXY-5-(2-METHYL-2H-TETRAZOL-5-YL)ISOXAZOL-4-YL]PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 8000, Zn(OAc)2, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.85 Å R-free 0.234
1M5B X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH 2-Me-Tet-AMPA AT 1.85 A RESOLUTION. Deposited 2002-07-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：flop ligand binding core (S1S2J) Chain B 653–796（144 aa） Fragment：flop ligand binding core (S1S2J)	Not recorded	ZN ZINC ION × 4 BN1 (S)-2-AMINO-3-[3-HYDROXY-5-(2-METHYL-2H-TETRAZOL-5-YL)ISOXAZOL-4-YL]PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 8000, Zn(OAc)2, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.85 Å R-free 0.234
1M5B X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH 2-Me-Tet-AMPA AT 1.85 A RESOLUTION. Deposited 2002-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：flop ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：flop ligand binding core (S1S2J) Chain B 413–527（115 aa） Fragment：flop ligand binding core (S1S2J) Chain B 653–796（144 aa） Fragment：flop ligand binding core (S1S2J) Chain C 413–527（115 aa） Fragment：flop ligand binding core (S1S2J) Chain C 653–796（144 aa） Fragment：flop ligand binding core (S1S2J)	Not recorded	ZN ZINC ION × 5 BN1 (S)-2-AMINO-3-[3-HYDROXY-5-(2-METHYL-2H-TETRAZOL-5-YL)ISOXAZOL-4-YL]PROPIONIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 8000, Zn(OAc)2, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.85 Å R-free 0.234
1M5C X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH Br-HIBO AT 1.65 A RESOLUTION Deposited 2002-07-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：flop ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：flop ligand binding core (S1S2J)	Not recorded	BRH (S)-2-AMINO-3-(4-BROMO-3-HYDROXY-ISOXAZOL-5-YL)PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；PEG 1450, Li2SO4, phosphate-citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.65 Å R-free 0.221
1M5D X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J-Y702F) IN COMPLEX WITH Br-HIBO AT 1.73 A RESOLUTION Deposited 2002-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain A 653–796（144 aa） Fragment：flop ligand binding core (S1S2J-Y702F)	Mutation：Y190F Mutation：Y190F	SO4 SULFATE ION × 4 BRH (S)-2-AMINO-3-(4-BROMO-3-HYDROXY-ISOXAZOL-5-YL)PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；PEG 3350, Li2SO4, phosphate-citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.73 Å R-free 0.215
1M5E X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH ACPA AT 1.46 A RESOLUTION Deposited 2002-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GluR2-flop ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：GluR2-flop ligand binding core (S1S2J) Chain C 413–527（115 aa） Fragment：GluR2-flop ligand binding core (S1S2J) Chain C 653–796（144 aa） Fragment：GluR2-flop ligand binding core (S1S2J)	Not recorded	ZN ZINC ION × 4 AM1 (S)-2-AMINO-3-(3-CARBOXY-5-METHYLISOXAZOL-4-YL)PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 8000, Zn(OAc)2, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.46 Å R-free 0.216
1M5E X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH ACPA AT 1.46 A RESOLUTION Deposited 2002-07-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：GluR2-flop ligand binding core (S1S2J) Chain B 653–796（144 aa） Fragment：GluR2-flop ligand binding core (S1S2J)	Not recorded	ZN ZINC ION × 8 AM1 (S)-2-AMINO-3-(3-CARBOXY-5-METHYLISOXAZOL-4-YL)PROPIONIC ACID × 2 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 8000, Zn(OAc)2, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.46 Å R-free 0.216
1M5E X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH ACPA AT 1.46 A RESOLUTION Deposited 2002-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：GluR2-flop ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：GluR2-flop ligand binding core (S1S2J) Chain B 413–527（115 aa） Fragment：GluR2-flop ligand binding core (S1S2J) Chain B 653–796（144 aa） Fragment：GluR2-flop ligand binding core (S1S2J) Chain C 413–527（115 aa） Fragment：GluR2-flop ligand binding core (S1S2J) Chain C 653–796（144 aa） Fragment：GluR2-flop ligand binding core (S1S2J)	Not recorded	ZN ZINC ION × 8 AM1 (S)-2-AMINO-3-(3-CARBOXY-5-METHYLISOXAZOL-4-YL)PROPIONIC ACID × 3 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 8000, Zn(OAc)2, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.46 Å R-free 0.216
1M5F X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J-Y702F) IN COMPLEX WITH ACPA AT 1.95 A RESOLUTION Deposited 2002-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain A 653–796（144 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain C 413–527（115 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain C 653–796（144 aa） Fragment：flop ligand binding core (S1S2J-Y702F)	Mutation：Y190F Mutation：Y190F Mutation：Y190F Mutation：Y190F	ZN ZINC ION × 2 AM1 (S)-2-AMINO-3-(3-CARBOXY-5-METHYLISOXAZOL-4-YL)PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 8000, Zn(OAc)2, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.230
1M5F X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J-Y702F) IN COMPLEX WITH ACPA AT 1.95 A RESOLUTION Deposited 2002-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain B 653–796（144 aa） Fragment：flop ligand binding core (S1S2J-Y702F)	Mutation：Y190F Mutation：Y190F	ZN ZINC ION × 8 AM1 (S)-2-AMINO-3-(3-CARBOXY-5-METHYLISOXAZOL-4-YL)PROPIONIC ACID × 2 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 8000, Zn(OAc)2, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.230
1M5F X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J-Y702F) IN COMPLEX WITH ACPA AT 1.95 A RESOLUTION Deposited 2002-07-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain A 653–796（144 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain B 413–527（115 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain B 653–796（144 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain C 413–527（115 aa） Fragment：flop ligand binding core (S1S2J-Y702F) Chain C 653–796（144 aa） Fragment：flop ligand binding core (S1S2J-Y702F)	Mutation：Y190F Mutation：Y190F Mutation：Y190F Mutation：Y190F Mutation：Y190F Mutation：Y190F	ZN ZINC ION × 6 AM1 (S)-2-AMINO-3-(3-CARBOXY-5-METHYLISOXAZOL-4-YL)PROPIONIC ACID × 3 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 8000, Zn(OAc)2, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.230
1MM6 crystal structure of the GluR2 ligand binding core (S1S2J) in complex with quisqualate in a non zinc crystal form at 2.15 angstroms resolution Deposited 2002-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	SO4 SULFATE ION × 3 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；PEG 8K, ammonium sulfate, sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.15 Å R-free 0.237
1MM7 Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Quisqualate in a Zinc Crystal Form at 1.65 Angstroms Resolution Deposited 2002-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；PEG 8K, zinc acetate, sodium acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.65 Å R-free 0.237
1MM7 Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Quisqualate in a Zinc Crystal Form at 1.65 Angstroms Resolution Deposited 2002-09-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；PEG 8K, zinc acetate, sodium acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.65 Å R-free 0.237
1MQD X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.46 A resolution. Crystallization in the presence of lithium sulfate. Deposited 2002-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain A 653–794（142 aa） Fragment：GluR2-flop ligand-binding core (S1S2J)	Not recorded	SO4 SULFATE ION × 2 SHI (S)-2-AMINO-3-(3-HYDROXY-ISOXAZOL-4-YL)PROPIONIC ACID × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；279 K；20% PEG 8000, 0.1M lithium sulfate, 0.1M cacodylate, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.46 Å R-free 0.192
1MQD X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.46 A resolution. Crystallization in the presence of lithium sulfate. Deposited 2002-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain B 653–794（142 aa） Fragment：GluR2-flop ligand-binding core (S1S2J)	Not recorded	SO4 SULFATE ION × 2 SHI (S)-2-AMINO-3-(3-HYDROXY-ISOXAZOL-4-YL)PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；279 K；20% PEG 8000, 0.1M lithium sulfate, 0.1M cacodylate, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.46 Å R-free 0.192
1MQD X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.46 A resolution. Crystallization in the presence of lithium sulfate. Deposited 2002-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain C 653–794（142 aa） Fragment：GluR2-flop ligand-binding core (S1S2J)	Not recorded	SHI (S)-2-AMINO-3-(3-HYDROXY-ISOXAZOL-4-YL)PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；279 K；20% PEG 8000, 0.1M lithium sulfate, 0.1M cacodylate, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.46 Å R-free 0.192
1MQD X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.46 A resolution. Crystallization in the presence of lithium sulfate. Deposited 2002-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain D 653–794（142 aa） Fragment：GluR2-flop ligand-binding core (S1S2J)	Not recorded	SO4 SULFATE ION × 2 SHI (S)-2-AMINO-3-(3-HYDROXY-ISOXAZOL-4-YL)PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；279 K；20% PEG 8000, 0.1M lithium sulfate, 0.1M cacodylate, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.46 Å R-free 0.192
1MQG Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Iodo-Willardiine at 2.15 Angstroms Resolution Deposited 2002-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain B 413–527（115 aa） Fragment：ligand binding core (S1S2J)	Not recorded	SO4 SULFATE ION × 2 IWD 2-AMINO-3-(5-IODO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；277 K；PEG 1000, Phosphate-citrate buffer, Li sulfate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.15 Å R-free 0.233
1MQH Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Bromo-Willardiine at 1.8 Angstroms Resolution Deposited 2002-09-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Not recorded	BWD 2-AMINO-3-(5-BROMO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；PEG 8K, ammonium sulfate, Na Acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.231
1MQI Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Fluoro-Willardiine at 1.35 Angstroms Resolution Deposited 2002-09-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J)	Not recorded	FWD 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；PEG 8K, NaCl, Na Citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.35 Å R-free 0.218
1MQJ Crystal structure of the GluR2 ligand binding core (S1S2J) in complex with willardiine at 1.65 angstroms resolution Deposited 2002-09-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J)	Not recorded	ZN ZINC ION × 2 HWD 2-AMINO-3-(2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；PEG 5K MME, Na Citrate, zinc acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.65 Å R-free 0.229
1MS7 X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.97 A resolution, Crystallization in the presence of zinc acetate Deposited 2002-09-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain A 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain C 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain C 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J)	Not recorded	ZN ZINC ION × 2 SHI (S)-2-AMINO-3-(3-HYDROXY-ISOXAZOL-4-YL)PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；17% PEG 8000, 0.05M zinc acetate, 0.1M cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.97 Å R-free 0.213
1MS7 X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.97 A resolution, Crystallization in the presence of zinc acetate Deposited 2002-09-19	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain B 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J)	Not recorded	ZN ZINC ION × 8 SHI (S)-2-AMINO-3-(3-HYDROXY-ISOXAZOL-4-YL)PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；17% PEG 8000, 0.05M zinc acetate, 0.1M cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.97 Å R-free 0.213
1MS7 X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.97 A resolution, Crystallization in the presence of zinc acetate Deposited 2002-09-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain A 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain B 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain B 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain C 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain C 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J)	Not recorded	ZN ZINC ION × 6 SHI (S)-2-AMINO-3-(3-HYDROXY-ISOXAZOL-4-YL)PROPIONIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；17% PEG 8000, 0.05M zinc acetate, 0.1M cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.97 Å R-free 0.213
1MXU CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) in complex with bromo-willardiine (Control for the crystal titration experiments) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3 BWD 2-AMINO-3-(5-BROMO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8K, ammonium sulfate, zinc acetate, BrW and sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.234
1MXU CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) in complex with bromo-willardiine (Control for the crystal titration experiments) Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4 BWD 2-AMINO-3-(5-BROMO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8K, ammonium sulfate, zinc acetate, BrW and sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.234
1MXU CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) in complex with bromo-willardiine (Control for the crystal titration experiments) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5 BWD 2-AMINO-3-(5-BROMO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8K, ammonium sulfate, zinc acetate, BrW and sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.234
1MXV crystal titration experiments (AMPA co-crystals soaked in 10 mM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.95 Å R-free 0.248
1MXV crystal titration experiments (AMPA co-crystals soaked in 10 mM BrW) Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.95 Å R-free 0.248
1MXV crystal titration experiments (AMPA co-crystals soaked in 10 mM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.95 Å R-free 0.248
1MXW crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.252
1MXW crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW) Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.252
1MXW crystal titration experiments (AMPA co-crystals soaked in 1 mM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.252
1MXX crystal titration experiments (AMPA co-crystals soaked in 100 uM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.250
1MXX crystal titration experiments (AMPA co-crystals soaked in 100 uM BrW) Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.250
1MXX crystal titration experiments (AMPA co-crystals soaked in 100 uM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.250
1MXY crystal titration experiments (AMPA co-crystals soaked in 10 uM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.95 Å R-free 0.259
1MXY crystal titration experiments (AMPA co-crystals soaked in 10 uM BrW) Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.95 Å R-free 0.259
1MXY crystal titration experiments (AMPA co-crystals soaked in 10 uM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.95 Å R-free 0.259
1MXZ crystal titration experiments (AMPA co-crystals soaked in 1 uM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.256
1MXZ crystal titration experiments (AMPA co-crystals soaked in 1 uM BrW) Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.256
1MXZ crystal titration experiments (AMPA co-crystals soaked in 1 uM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.256
1MY0 crystal titration experiments (AMPA co-crystals soaked in 100 nM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.249
1MY0 crystal titration experiments (AMPA co-crystals soaked in 100 nM BrW) Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.249
1MY0 crystal titration experiments (AMPA co-crystals soaked in 100 nM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.249
1MY1 crystal titration experiments (AMPA co-crystals soaked in 10 nM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.248
1MY1 crystal titration experiments (AMPA co-crystals soaked in 10 nM BrW) Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.248
1MY1 crystal titration experiments (AMPA co-crystals soaked in 10 nM BrW) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.248
1MY2 crystal titration experiment (AMPA complex control) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.244
1MY2 crystal titration experiment (AMPA complex control) Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.244
1MY2 crystal titration experiment (AMPA complex control) Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.244
1MY3 crystal structure of glutamate receptor ligand-binding core in complex with bromo-willardiine in the Zn crystal form Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3 BWD 2-AMINO-3-(5-BROMO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, ammonium sulfate, zinc acetate and sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.75 Å R-free 0.255
1MY3 crystal structure of glutamate receptor ligand-binding core in complex with bromo-willardiine in the Zn crystal form Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4 BWD 2-AMINO-3-(5-BROMO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, ammonium sulfate, zinc acetate and sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.75 Å R-free 0.255
1MY4 crystal structure of glutamate receptor ligand-binding core in complex with iodo-willardiine in the Zn crystal form Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3 IWD 2-AMINO-3-(5-IODO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG4K, ammonium sulfate, zinc acetate and Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.262
1MY4 crystal structure of glutamate receptor ligand-binding core in complex with iodo-willardiine in the Zn crystal form Deposited 2002-10-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4 IWD 2-AMINO-3-(5-IODO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG4K, ammonium sulfate, zinc acetate and Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.262
1MY4 crystal structure of glutamate receptor ligand-binding core in complex with iodo-willardiine in the Zn crystal form Deposited 2002-10-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–796（144 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 5 IWD 2-AMINO-3-(5-IODO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG4K, ammonium sulfate, zinc acetate and Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.262
1N0T X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with the antagonist (S)-ATPO at 2.1 A resolution. Deposited 2002-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J). Chain A 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J). Chain C 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J). Chain C 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J).	Not recorded	AT1 (S)-2-AMINO-3-(5-TERT-BUTYL-3-(PHOSPHONOMETHOXY)-4-ISOXAZOLYL)PROPIONIC ACID × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；279 K；PEG 3350, AMMONIUM SULFATE, SODIUM ACETATE pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.10 Å R-free 0.245
1N0T X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with the antagonist (S)-ATPO at 2.1 A resolution. Deposited 2002-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J). Chain B 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J). Chain D 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J). Chain D 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J).	Not recorded	AT1 (S)-2-AMINO-3-(5-TERT-BUTYL-3-(PHOSPHONOMETHOXY)-4-ISOXAZOLYL)PROPIONIC ACID × 2 SO4 SULFATE ION × 2 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；279 K；PEG 3350, AMMONIUM SULFATE, SODIUM ACETATE pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.10 Å R-free 0.245
1NNK X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.85 A resolution. Crystallization with zinc ions. Deposited 2003-01-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain A 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J)	Not recorded	ZN ZINC ION × 4 CL CHLORIDE ION × 2 CE2 3-(5-TERT-BUTYL-3-OXIDOISOXAZOL-4-YL)-L-ALANINATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；zinc acetate, cacodylate, PEG8000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.85 Å R-free 0.245
1NNP X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.9 A resolution. Crystallization without zinc ions. Deposited 2003-01-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GluR2-flop ligand-binding core (S1S2J) Chain B 653–796（144 aa） Fragment：GluR2-flop ligand-binding core (S1S2J)	Not recorded	SO4 SULFATE ION × 2 CE2 3-(5-TERT-BUTYL-3-OXIDOISOXAZOL-4-YL)-L-ALANINATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；279 K；ammonium sulfate, PEG8000, sodium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.90 Å R-free 0.216
1P1N GluR2 Ligand Binding Core (S1S2J) Mutant L650T in Complex with Kainate Deposited 2003-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Mutation：L138T Mutation：L138T	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；PEG 4000, ammonium sulfate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.60 Å R-free 0.252
1P1O Crystal structure of the GluR2 ligand-binding core (S1S2J) mutant L650T in complex with quisqualate Deposited 2003-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Mutation：L138T Mutation：L138T	SO4 SULFATE ION × 4 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；PEG4000, ammonium sulfate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.60 Å R-free 0.235
1P1Q Crystal structure of the GluR2 ligand binding core (S1S2J) L650T mutant in complex with AMPA Deposited 2003-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：ligand binding core (S1S2J) Chain C 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain C 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Mutation：L138T Mutation：L138T Mutation：L138T Mutation：L138T	ZN ZINC ION × 3 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, cacodylate, zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.270
1P1Q Crystal structure of the GluR2 ligand binding core (S1S2J) L650T mutant in complex with AMPA Deposited 2003-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain B 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Mutation：L138T Mutation：L138T	ZN ZINC ION × 4 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG8000, cacodylate, zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.270
1P1U Crystal structure of the GluR2 ligand-binding core (S1S2J) L650T mutant in complex with AMPA (ammonium sulfate crystal form) Deposited 2003-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：ligand binding core (S1S2J) Chain B 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain B 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Mutation：L138T Mutation：L138T Mutation：L138T Mutation：L138T	SO4 SULFATE ION × 1 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；PEG4000, ammonium sulfate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.271
1P1W Crystal structure of the GluR2 ligand-binding core (S1S2J) with the L483Y and L650T mutations and in complex with AMPA Deposited 2003-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：ligand binding core (S1S2J) Chain B 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain B 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Mutation：L94Y,L138T Mutation：L94Y,L138T Mutation：L94Y,L138T Mutation：L94Y,L138T	SO4 SULFATE ION × 2 AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLEPROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；PEG4000, ammonium sulfate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.264
1SYH X-RAY STRUCTURE OF THE GLUR2 LIGAND-BINDING CORE (S1S2J) IN COMPLEX WITH (S)-CPW399 AT 1.85 A RESOLUTION. Deposited 2004-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–796（384 aa） Fragment：GLUR2-FLOP LIGAND-BINDING CORE (S1S2J)	Not recorded	CPW (S)-2-AMINO-3-(1,3,5,7-PENTAHYDRO-2,4-DIOXO-CYCLOPENTA[E]PYRIMIDIN-1-YL) PROIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；PEG8000, cacodylate, (NH4)2SO4 , pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 1.80 Å R-free 0.199
1SYI X-RAY STRUCTURE OF THE Y702F MUTANT OF THE GLUR2 LIGAND-BINDING CORE (S1S2J) IN COMPLEX WITH (S)-CPW399 AT 2.1 A RESOLUTION. Deposited 2004-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–796（384 aa） Fragment：GLUR2-FLOP LIGAND-BINDING CORE (S1S2J) Chain B 413–796（384 aa） Fragment：GLUR2-FLOP LIGAND-BINDING CORE (S1S2J)	Mutation：Y702F Mutation：Y702F	CPW (S)-2-AMINO-3-(1,3,5,7-PENTAHYDRO-2,4-DIOXO-CYCLOPENTA[E]PYRIMIDIN-1-YL) PROIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；280 K；PEG8000, CACODYLATE, (NH4)2SO4, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.10 Å R-free 0.254
1WVJ Exploring the GluR2 ligand-binding core in complex with the bicyclic AMPA analogue (S)-4-AHCP Deposited 2004-12-15	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Not recorded	SO4 SULFATE ION × 4 IBC 3-(3-HYDROXY-7,8-DIHYDRO-6H-CYCLOHEPTA[D]ISOXAZOL-4-YL)-L-ALANINE × 2 GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；PEG 3350, phosphate-citrate buffer, lithium sulfate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.75 Å R-free 0.214
1XHY X-ray structure of the Y702F mutant of the GluR2 ligand-binding core (S1S2J) in complex with kainate at 1.85 A resolution Deposited 2004-09-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GluR2 flop ligand-binding core (S1S2J), UNP residues 413-527 and 653-796 Chain A 653–796（144 aa） Fragment：GluR2 flop ligand-binding core (S1S2J), UNP residues 413-527 and 653-796	Mutation：Y702F Mutation：Y702F	SO4 SULFATE ION × 10 KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；280 K；PEG1000, Li2SO4, cacodylate , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 1.85 Å R-free 0.207
2AIX X-ray structure of the GLUR2 ligand-binding core (S1S2J) in complex with (s)-thio-atpa at 2.2 a resolution. Deposited 2005-08-01	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GLUR2-FLOP LIGAND-BINDING CORE (S1S2J). Chain A 653–796（144 aa） Fragment：GLUR2-FLOP LIGAND-BINDING CORE (S1S2J).	Not recorded	U1K (S)-2-AMINO-3-(3-HYDROXY-5-TERT-BUTYLISOTHIAZOL-4-YL) PROPRIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；279 K；SODIUM CHLORIDE, CACODYLATE, PEG 8000, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.17 Å R-free 0.230
2AL4 CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH quisqualate and CX614. Deposited 2005-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：ligand binding core (S1S2J) Chain B 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain B 653–796（144 aa） Fragment：ligand binding core (S1S2J) Chain F 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain F 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker.	ZN ZINC ION × 5 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 3 CX6 2,3,6A,7,8,9-HEXAHYDRO-11H-[1,4]DIOXINO[2,3-G]PYRROLO[2,1-B][1,3]BENZOXAZIN-11-ONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；10-14% PEG8000, 0.1-0.15 M Zinc acetate, 0.1 M sodium acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.223
2AL4 CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH quisqualate and CX614. Deposited 2005-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain C 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain C 653–796（144 aa） Fragment：ligand binding core (S1S2J) Chain D 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain D 653–796（144 aa） Fragment：ligand binding core (S1S2J) Chain E 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain E 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker.	ZN ZINC ION × 5 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 3 CX6 2,3,6A,7,8,9-HEXAHYDRO-11H-[1,4]DIOXINO[2,3-G]PYRROLO[2,1-B][1,3]BENZOXAZIN-11-ONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；10-14% PEG8000, 0.1-0.15 M Zinc acetate, 0.1 M sodium acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.223
2AL5 Crystal structure of the GluR2 ligand binding core (S1S2J) in complex with fluoro-willardiine and aniracetam Deposited 2005-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain A 653–796（144 aa） Fragment：ligand binding core (S1S2J) Chain B 413–527（115 aa） Fragment：ligand binding core (S1S2J) Chain B 653–796（144 aa） Fragment：ligand binding core (S1S2J)	Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. Mutation：The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker.	FWD 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2 4MP 1-(4-METHOXYBENZOYL)-2-PYRROLIDINONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；12-14% PEG 8000, 0.25-0.35 M ammonium sulfate and 0.1 M sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.65 Å R-free 0.220
2ANJ Crystal Structure of the Glur2 Ligand Binding Core (S1S2J-Y450W) Mutant in Complex With the Partial Agonist Kainic Acid at 2.1 A Resolution Deposited 2005-08-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand Binding Core Chain A 653–796（144 aa） Fragment：Ligand Binding Core	Mutation：Y61W Mutation：Y61W	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；279 K；PEG 8000, Cacodylate, Lithium Sulphate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K, pH 6.50	Resolution 2.10 Å R-free 0.248
2CMO The structure of a mixed glur2 ligand-binding core dimer in complex with (s)-glutamate and the antagonist (s)-ns1209 Deposited 2006-05-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：RESIDUES 413-527,653-796 Chain A 653–796（144 aa） Fragment：RESIDUES 413-527,653-796 Chain B 413–527（115 aa） Fragment：RESIDUES 413-527,653-796 Chain B 653–796（144 aa） Fragment：RESIDUES 413-527,653-796	Not recorded	SO4 SULFATE ION × 4 M1L 2-({[(3E)-5-{4-[(DIMETHYLAMINO)(DIHYDROXY)-LAMBDA~4~-SULFANYL]PHENYL}-8-METHYL-2-OXO-6,7,8,9-TETRAHYDRO-1H-PYRROLO[3,2-H]ISOQUINOLIN-3(2H)-YLIDENE]AMINO}OXY)-4-HYDROXYBUTANOIC ACID × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.50	Resolution 2.65 Å R-free 0.281
2GFE Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution Deposited 2006-03-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–795（143 aa） Chain C 413–527（115 aa） Chain C 653–795（143 aa）	Mutation：A476E S673D Mutation：A476E S673D Mutation：A476E S673D Mutation：A476E S673D	ZN ZINC ION × 3 GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；1 to 1 mixture of: Reservoir: 14% PEG 8K; 0.1M Na Acetate; 0.1 M Zn Acetate. Protein: 10 mg/ml 0.01 M Na HEPES pH 7.0; 0.02 M NaCl; 0.01 M Na Glutamate; 0.001 M EDTA, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.54 Å R-free 0.227
2GFE Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution Deposited 2006-03-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Chain B 653–795（143 aa）	Mutation：A476E S673D Mutation：A476E S673D	ZN ZINC ION × 2 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；1 to 1 mixture of: Reservoir: 14% PEG 8K; 0.1M Na Acetate; 0.1 M Zn Acetate. Protein: 10 mg/ml 0.01 M Na HEPES pH 7.0; 0.02 M NaCl; 0.01 M Na Glutamate; 0.001 M EDTA, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.54 Å R-free 0.227
2GFE Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution Deposited 2006-03-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 413–527（115 aa） Chain A 653–795（143 aa） Chain B 413–527（115 aa） Chain B 653–795（143 aa） Chain C 413–527（115 aa） Chain C 653–795（143 aa）	Mutation：A476E S673D Mutation：A476E S673D Mutation：A476E S673D Mutation：A476E S673D Mutation：A476E S673D Mutation：A476E S673D	ZN ZINC ION × 5 GLU GLUTAMIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；1 to 1 mixture of: Reservoir: 14% PEG 8K; 0.1M Na Acetate; 0.1 M Zn Acetate. Protein: 10 mg/ml 0.01 M Na HEPES pH 7.0; 0.02 M NaCl; 0.01 M Na Glutamate; 0.001 M EDTA, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.54 Å R-free 0.227
2GFE Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution Deposited 2006-03-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–795（143 aa） Chain B 413–527（115 aa） Chain B 653–795（143 aa）	Mutation：A476E S673D Mutation：A476E S673D Mutation：A476E S673D Mutation：A476E S673D	ZN ZINC ION × 3 GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；1 to 1 mixture of: Reservoir: 14% PEG 8K; 0.1M Na Acetate; 0.1 M Zn Acetate. Protein: 10 mg/ml 0.01 M Na HEPES pH 7.0; 0.02 M NaCl; 0.01 M Na Glutamate; 0.001 M EDTA, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.54 Å R-free 0.227
2I3V Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant Deposited 2006-08-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 2 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；0.1 M CACODYLATE, 18% PEG 8000, 0.2 M ZINC ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 2.40 Å R-free 0.281
2I3V Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant Deposited 2006-08-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；0.1 M CACODYLATE, 18% PEG 8000, 0.2 M ZINC ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 2.40 Å R-free 0.281
2I3V Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant Deposited 2006-08-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；0.1 M CACODYLATE, 18% PEG 8000, 0.2 M ZINC ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 2.40 Å R-free 0.281
2I3V Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant Deposited 2006-08-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain D 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；0.1 M CACODYLATE, 18% PEG 8000, 0.2 M ZINC ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 2.40 Å R-free 0.281
2I3V Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant Deposited 2006-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain D 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain D 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 7 GLU GLUTAMIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；0.1 M CACODYLATE, 18% PEG 8000, 0.2 M ZINC ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 2.40 Å R-free 0.281
2I3V Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant Deposited 2006-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain D 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain D 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4 GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；0.1 M CACODYLATE, 18% PEG 8000, 0.2 M ZINC ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 2.40 Å R-free 0.281
2I3V Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant Deposited 2006-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain C 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 3 GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；0.1 M CACODYLATE, 18% PEG 8000, 0.2 M ZINC ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 2.40 Å R-free 0.281
2I3V Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of G725C mutant Deposited 2006-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 8 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain D 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain D 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Not recorded	ZN ZINC ION × 4 GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；0.1 M CACODYLATE, 18% PEG 8000, 0.2 M ZINC ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 2.40 Å R-free 0.281
2I3W Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of S729C mutant Deposited 2006-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Mutation：G729C Mutation：G729C	GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；0.1 M CITRATE 20% PEG 3000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.30 Å R-free 0.284
2I3W Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of S729C mutant Deposited 2006-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Mutation：G729C Mutation：G729C	GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；0.1 M CITRATE 20% PEG 3000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.30 Å R-free 0.284
2I3W Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor: Structure of S729C mutant Deposited 2006-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain A 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 413–527（115 aa） Fragment：LIGAND BINDING CORE (S1S2J) Chain B 653–794（142 aa） Fragment：LIGAND BINDING CORE (S1S2J)	Mutation：G729C Mutation：G729C Mutation：G729C Mutation：G729C	GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；0.1 M CITRATE 20% PEG 3000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.30 Å R-free 0.284
2P2A X-ray structure of the GluR2 ligand binding core (S1S2J) in complex with 2-Bn-tet-AMPA at 2.26A resolution Deposited 2007-03-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：GluR2-Flop ligand-binding core (Residues 413-527, 653-796) Chain A 653–796（144 aa） Fragment：GluR2-Flop ligand-binding core (Residues 413-527, 653-796) Chain B 413–527（115 aa） Fragment：GluR2-Flop ligand-binding core (Residues 413-527, 653-796) Chain B 653–796（144 aa） Fragment：GluR2-Flop ligand-binding core (Residues 413-527, 653-796)	Not recorded	SO4 SULFATE ION × 3 GLU GLUTAMIC ACID × 1 MP9 2-AMINO-3-[3-HYDROXY-5-(2-BENZYL-2H-5-TETRAZOLYL)-4-ISOXAZOLYL]-PROPIONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；PEG4000, Sodium Acetate, Ammonium Sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.26 Å R-free 0.273
2XX7 Crystal structure of 1-(4-(1-pyrrolidinylcarbonyl)phenyl)-3-(trifluoromethyl)-4,5,6,7-tetrahydro-1H-indazole in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 2.2A resolution. Deposited 2010-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-795 Chain A 653–795（143 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-795 Chain C 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-795 Chain C 653–795（143 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-795	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 1ND 1-[4-(1-PYRROLIDINYLCARBONYL)PHENYL]-3-(TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOLE × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.218
2XX7 Crystal structure of 1-(4-(1-pyrrolidinylcarbonyl)phenyl)-3-(trifluoromethyl)-4,5,6,7-tetrahydro-1H-indazole in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 2.2A resolution. Deposited 2010-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-795 Chain B 653–795（143 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-795	Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 1ND 1-[4-(1-PYRROLIDINYLCARBONYL)PHENYL]-3-(TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOLE × 2 SO4 SULFATE ION × 2 ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.218
2XX8 Crystal structure of N,N-dimethyl-4-(3-(trifluoromethyl)-4,5,6,7- tetrahydro-1H-indazol-1-yl)benzamide in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 2.2A resolution. Deposited 2010-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain A 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain C 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain C 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 1NE N,N-DIMETHYL-4-[3-(TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOL-1-YL]BENZAMIDE × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.55 Å R-free 0.212
2XX8 Crystal structure of N,N-dimethyl-4-(3-(trifluoromethyl)-4,5,6,7- tetrahydro-1H-indazol-1-yl)benzamide in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 2.2A resolution. Deposited 2010-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain B 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796	Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 1NE N,N-DIMETHYL-4-[3-(TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOL-1-YL]BENZAMIDE × 2 SO4 SULFATE ION × 2 ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.55 Å R-free 0.212
2XX9 Crystal structure of 1-((2-fluoro-4-(3-(trifluoromethyl)-4,5,6,7- tetrahydro-1H-indazol-1-yl)phenyl)methyl)-2-pyrrolidinone in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 2.2A resolution. Deposited 2010-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain B 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796	Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 1NF N,N-DIMETHYL-4-[3-(TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOL-1-YL]BENZAMIDE × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.97 Å R-free 0.224
2XX9 Crystal structure of 1-((2-fluoro-4-(3-(trifluoromethyl)-4,5,6,7- tetrahydro-1H-indazol-1-yl)phenyl)methyl)-2-pyrrolidinone in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 2.2A resolution. Deposited 2010-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain A 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain C 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain C 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 1NF N,N-DIMETHYL-4-[3-(TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOL-1-YL]BENZAMIDE × 1 SO4 SULFATE ION × 1 ZN ZINC ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.97 Å R-free 0.224
2XXH Crystal structure of 1-(4-(2-oxo-2-(1-pyrrolidinyl)ethyl)phenyl)-3-(trifluoromethyl)-4,5,6,7-tetrahydro-1H-indazole in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 1.5A resolution. Deposited 2010-11-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain B 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796	Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 1NG 1-{4-[2-OXO-2-(1-PYRROLIDINYL)ETHYL]PHENYL}-3-( TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOLE × 2 SO4 SULFATE ION × 2 ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.50 Å R-free 0.218
2XXH Crystal structure of 1-(4-(2-oxo-2-(1-pyrrolidinyl)ethyl)phenyl)-3-(trifluoromethyl)-4,5,6,7-tetrahydro-1H-indazole in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 1.5A resolution. Deposited 2010-11-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain A 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain C 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain C 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 1NG 1-{4-[2-OXO-2-(1-PYRROLIDINYL)ETHYL]PHENYL}-3-( TRIFLUOROMETHYL)-4,5,6,7-TETRAHYDRO-1H-INDAZOLE × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.50 Å R-free 0.218
2XXI Crystal structure of 1-((4-(3-(trifluoromethyl)-6,7-dihydropyrano(4,3- c(pyrazol-1(4H)-yl)phenyl)methyl)-2-pyrrolidinone in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 1.6A resolution. Deposited 2010-11-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain A 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain C 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain C 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 JAC 1-({4-[3-(TRIFLUOROMETHYL)-6,7-DIHYDROPYRANO[4,3-C]PYRAZOL-1(4H)-YL]PHENYL}METHYL)-2-PYRROLIDINONE × 1 SO4 SULFATE ION × 1 ZN ZINC ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.60 Å R-free 0.208
2XXI Crystal structure of 1-((4-(3-(trifluoromethyl)-6,7-dihydropyrano(4,3- c(pyrazol-1(4H)-yl)phenyl)methyl)-2-pyrrolidinone in complex with the ligand binding domain of the Rat GluA2 receptor and glutamate at 1.6A resolution. Deposited 2010-11-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796 Chain B 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, RESIDUES 413-527,653-796	Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 JAC 1-({4-[3-(TRIFLUOROMETHYL)-6,7-DIHYDROPYRANO[4,3-C]PYRAZOL-1(4H)-YL]PHENYL}METHYL)-2-PYRROLIDINONE × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.60 Å R-free 0.208
3B6Q Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) Mutant T686A in Complex with Glutamate at 2.0 Resolution Deposited 2007-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Mutation：T686A Mutation：T686A	SO4 SULFATE ION × 2 GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；293 K；0.1 M Tris-HCl, 0.15-0.2 M lithium sulfate, 18-21% PEG4000, pH 8.5, VAPOR DIFFUSION, temperature 293K	Resolution 2.00 Å R-free 0.222
3B6T Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) T686A Mutant in Complex with Quisqualate at 2.1 Resolution Deposited 2007-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Mutation：T686A Mutation：T686A	SO4 SULFATE ION × 2 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.1 M Tris-HCl, 0.15-0.2 M lithium sulfate, 18-21% PEG4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.10 Å R-free 0.274
3B6W Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) T686S Mutant in Complex with Glutamate at 1.7 Resolution Deposited 2007-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa） Chain C 413–527（115 aa） Chain C 653–796（144 aa）	Mutation：T686S Mutation：T686S Mutation：T686S Mutation：T686S	SO4 SULFATE ION × 3 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.1 M Tris-HCl, 0.15-0.2 M lithium sulfate, 18-21% PEG4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.70 Å R-free 0.260
3B6W Crystal Structure of the GLUR2 Ligand Binding Core (S1S2J) T686S Mutant in Complex with Glutamate at 1.7 Resolution Deposited 2007-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Chain B 653–796（144 aa） Chain D 413–527（115 aa） Chain D 653–796（144 aa）	Mutation：T686S Mutation：T686S Mutation：T686S Mutation：T686S	SO4 SULFATE ION × 1 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.1 M Tris-HCl, 0.15-0.2 M lithium sulfate, 18-21% PEG4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.70 Å R-free 0.260
3B7D Crystal structure of the GLUR2 ligand binding core (HS1S2J) in complex with CNQX at 2.5 A resolution Deposited 2007-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–794（142 aa） Chain B 413–527（115 aa） Chain B 653–794（142 aa）	Not recorded	CNI 7-nitro-2,3-dioxo-2,3-dihydroquinoxaline-6-carbonitrile × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；40 mM Sodium citrate, 10 mM Ammonium sulfate, 1% PEG 400, pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.50 Å R-free 0.283
3B7D Crystal structure of the GLUR2 ligand binding core (HS1S2J) in complex with CNQX at 2.5 A resolution Deposited 2007-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Chain C 653–794（142 aa） Chain D 413–527（115 aa） Chain D 653–794（142 aa）	Not recorded	CNI 7-nitro-2,3-dioxo-2,3-dihydroquinoxaline-6-carbonitrile × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；40 mM Sodium citrate, 10 mM Ammonium sulfate, 1% PEG 400, pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.50 Å R-free 0.283
3B7D Crystal structure of the GLUR2 ligand binding core (HS1S2J) in complex with CNQX at 2.5 A resolution Deposited 2007-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 413–527（115 aa） Chain E 653–794（142 aa） Chain F 413–527（115 aa） Chain F 653–794（142 aa）	Not recorded	CNI 7-nitro-2,3-dioxo-2,3-dihydroquinoxaline-6-carbonitrile × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；40 mM Sodium citrate, 10 mM Ammonium sulfate, 1% PEG 400, pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.50 Å R-free 0.283
3B7D Crystal structure of the GLUR2 ligand binding core (HS1S2J) in complex with CNQX at 2.5 A resolution Deposited 2007-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 413–527（115 aa） Chain G 653–794（142 aa） Chain H 413–527（115 aa） Chain H 653–794（142 aa）	Not recorded	CNI 7-nitro-2,3-dioxo-2,3-dihydroquinoxaline-6-carbonitrile × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；40 mM Sodium citrate, 10 mM Ammonium sulfate, 1% PEG 400, pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.50 Å R-free 0.283
3BBR Crystal structure of the iGluR2 ligand binding core (S1S2J-N775S) in complex with a dimeric positive modulator as well as glutamate at 2.25 A resolution Deposited 2007-11-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding core Chain A 653–796（144 aa） Fragment：Ligand binding core Chain B 413–527（115 aa） Fragment：Ligand binding core Chain B 653–796（144 aa） Fragment：Ligand binding core	Mutation：N775S Mutation：N775S Mutation：N775S Mutation：N775S	SO4 SULFATE ION × 5 CL CHLORIDE ION × 1 GLU GLUTAMIC ACID × 2 BHY N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dimethanesulfonamide × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；0.3M ammonium sulfate, 0.1M sodium acetate, 25% PEG 4000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.25 Å R-free 0.231
3BFT Structure of the ligand-binding core of GluR2 in complex with the agonist (S)-TDPA at 2.25 A resolution Deposited 2007-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：residues 1-263 Chain A 653–796（144 aa） Fragment：residues 1-263 Chain C 413–527（115 aa） Fragment：residues 1-263 Chain C 653–796（144 aa） Fragment：residues 1-263	Not recorded	S2P (2S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid × 2 ZN ZINC ION × 2 NA SODIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 2000, cacodylate, zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.27 Å R-free 0.250
3BFT Structure of the ligand-binding core of GluR2 in complex with the agonist (S)-TDPA at 2.25 A resolution Deposited 2007-11-23	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：residues 1-263 Chain B 653–796（144 aa） Fragment：residues 1-263	Not recorded	S2P (2S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid × 2 ZN ZINC ION × 6 NA SODIUM ION × 2 CAC CACODYLATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 2000, cacodylate, zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.27 Å R-free 0.250
3BFU Structure of the ligand-binding core of GluR2 in complex with the agonist (R)-TDPA at 1.95 A resolution Deposited 2007-11-23	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：residues 1-263 Chain A 653–796（144 aa） Fragment：residues 1-263	Not recorded	R2P (2R)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 2000, cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.233
3BFU Structure of the ligand-binding core of GluR2 in complex with the agonist (R)-TDPA at 1.95 A resolution Deposited 2007-11-23	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：residues 1-263 Chain B 653–796（144 aa） Fragment：residues 1-263	Not recorded	R2P (2R)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 2000, cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.233
3BFU Structure of the ligand-binding core of GluR2 in complex with the agonist (R)-TDPA at 1.95 A resolution Deposited 2007-11-23	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Fragment：residues 1-263 Chain C 653–796（144 aa） Fragment：residues 1-263	Not recorded	R2P (2R)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 2000, cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.233
3BFU Structure of the ligand-binding core of GluR2 in complex with the agonist (R)-TDPA at 1.95 A resolution Deposited 2007-11-23	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 413–527（115 aa） Fragment：residues 1-263 Chain D 653–796（144 aa） Fragment：residues 1-263	Not recorded	R2P (2R)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；PEG 2000, cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.233
3BKI Crystal Structure of the GluR2 ligand binding core (S1S2J) in complex with FQX at 1.87 Angstroms Deposited 2007-12-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain P 413–527（115 aa） Chain P 653–796（144 aa）	Not recorded	FQX [1,2,5]oxadiazolo[3,4-g]quinoxaline-6,7(5H,8H)-dione 1-oxide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 1.87 Å R-free 0.221
3BKI Crystal Structure of the GluR2 ligand binding core (S1S2J) in complex with FQX at 1.87 Angstroms Deposited 2007-12-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Chain B 653–796（144 aa）	Not recorded	FQX [1,2,5]oxadiazolo[3,4-g]quinoxaline-6,7(5H,8H)-dione 1-oxide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 1.87 Å R-free 0.221
3BKI Crystal Structure of the GluR2 ligand binding core (S1S2J) in complex with FQX at 1.87 Angstroms Deposited 2007-12-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 413–527（115 aa） Chain C 653–796（144 aa）	Not recorded	FQX [1,2,5]oxadiazolo[3,4-g]quinoxaline-6,7(5H,8H)-dione 1-oxide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 1.87 Å R-free 0.221
3BKI Crystal Structure of the GluR2 ligand binding core (S1S2J) in complex with FQX at 1.87 Angstroms Deposited 2007-12-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 413–527（115 aa） Chain D 653–796（144 aa）	Not recorded	FQX [1,2,5]oxadiazolo[3,4-g]quinoxaline-6,7(5H,8H)-dione 1-oxide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP	Resolution 1.87 Å R-free 0.221
3DP6 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to glutamate Deposited 2008-07-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：S1S2 binding domain Chain A 653–796（144 aa） Fragment：S1S2 binding domain	Not recorded	ZN ZINC ION × 2 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；14-17% PEG 8000, 0.1-0.2 M Zn acetate, 0.1 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 1.55 Å R-free 0.244
3DP6 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to glutamate Deposited 2008-07-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：S1S2 binding domain Chain B 653–796（144 aa） Fragment：S1S2 binding domain	Not recorded	ZN ZINC ION × 2 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；14-17% PEG 8000, 0.1-0.2 M Zn acetate, 0.1 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 1.55 Å R-free 0.244
3DP6 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to glutamate Deposited 2008-07-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 413–527（115 aa） Fragment：S1S2 binding domain Chain C 653–796（144 aa） Fragment：S1S2 binding domain	Not recorded	ZN ZINC ION × 2 GLU GLUTAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；277 K；14-17% PEG 8000, 0.1-0.2 M Zn acetate, 0.1 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 6.50	Resolution 1.55 Å R-free 0.244
3H03 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to UBP277 Deposited 2009-04-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain A 653–794（142 aa） Fragment：UNP residues 414-527, 652-794 Chain B 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain B 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	UBP 3-[3-(2-carboxyethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]-L-alanine × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-16% PEG8K, 0.1-0.15 M Zn acetate, 0.25 M ammonium sulfate, 0.1 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.258
3H03 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to UBP277 Deposited 2009-04-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain D 653–794（142 aa） Fragment：UNP residues 414-527, 652-794 Chain G 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain G 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	UBP 3-[3-(2-carboxyethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]-L-alanine × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-16% PEG8K, 0.1-0.15 M Zn acetate, 0.25 M ammonium sulfate, 0.1 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.258
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain G 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain G 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 10 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain E 653–794（142 aa） Fragment：UNP residues 414-527, 652-794 Chain P 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain P 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 11 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain G 653–794（142 aa） Fragment：UNP residues 414-527, 652-794 Chain J 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain J 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 12 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain H 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain H 653–794（142 aa） Fragment：UNP residues 414-527, 652-794 Chain L 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain L 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain B 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain E 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain H 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain H 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain J 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain J 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain L 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain L 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain N 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain N 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain P 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain P 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H06 Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282 Deposited 2009-04-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 9 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain B 653–794（142 aa） Fragment：UNP residues 414-527, 652-794 Chain N 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain N 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.295
3H5V Crystal structure of the GluR2-ATD Deposited 2009-04-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 0–383（384 aa） Fragment：UNP residues 21-404 Chain B 0–383（384 aa） Fragment：UNP residues 21-404	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；14-16% PEG3350, 100mM TrisHCl, 10mM MgCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.33 Å R-free 0.235
3H5V Crystal structure of the GluR2-ATD Deposited 2009-04-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 0–383（384 aa） Fragment：UNP residues 21-404	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；14-16% PEG3350, 100mM TrisHCl, 10mM MgCl2, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.33 Å R-free 0.235
3H5W Crystal structure of the GluR2-ATD in space group P212121 without solvent Deposited 2009-04-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 0–383（384 aa） Fragment：UNP residues 21-404 Chain B 0–383（384 aa） Fragment：UNP residues 21-404	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；20% PEG3000, 100mM tri-sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.69 Å R-free 0.291
3H6T Crystal structure of the iGluR2 ligand-binding core (S1S2J-N754S) in complex with glutamate and cyclothiazide at 2.25 A resolution Deposited 2009-04-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain A 653–796（144 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain C 413–527（115 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain C 653–796（144 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796	Mutation：N754S Mutation：N754S Mutation：N754S Mutation：N754S	GLU GLUTAMIC ACID × 2 CYZ CYCLOTHIAZIDE × 2 ZN ZINC ION × 5 GOL GLYCEROL × 6 ACT ACETATE ION × 2 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；279 K；25 % PEG 4000, 0.3 M Zinc acetate, 0.1 M Cacodylate pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.25 Å R-free 0.228
3H6T Crystal structure of the iGluR2 ligand-binding core (S1S2J-N754S) in complex with glutamate and cyclothiazide at 2.25 A resolution Deposited 2009-04-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain B 653–796（144 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796	Mutation：N754S Mutation：N754S	GLU GLUTAMIC ACID × 2 CYZ CYCLOTHIAZIDE × 2 ZN ZINC ION × 10 GOL GLYCEROL × 6 CAC CACODYLATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；279 K；25 % PEG 4000, 0.3 M Zinc acetate, 0.1 M Cacodylate pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.25 Å R-free 0.228
3H6U Crystal structure of the iGluR2 ligand-binding core (S1S2J-N754S) in complex with glutamate and NS1493 at 1.85 A resolution Deposited 2009-04-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain A 653–796（144 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796	Mutation：N754S Mutation：N754S	GLU GLUTAMIC ACID × 2 NS3 (3S)-3-cyclopentyl-6-methyl-7-[(4-methylpiperazin-1-yl)sulfonyl]-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide × 2 SO4 SULFATE ION × 12 GOL GLYCEROL × 4 FLC CITRATE ANION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.5；279 K；25 % PEG 8000, 0.1 M Lithium sulfate, 0.1 M Phosphate-citrate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.85 Å R-free 0.215
3H6V Crystal structure of the iGluR2 ligand-binding core (S1S2J-N754S) in complex with glutamate and NS5206 at 2.10 A resolution Deposited 2009-04-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain A 653–796（144 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain B 413–527（115 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain B 653–796（144 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796	Mutation：N754S Mutation：N754S Mutation：N754S Mutation：N754S	GLU GLUTAMIC ACID × 2 NS6 (3R)-3-cyclopentyl-7-[(4-methylpiperazin-1-yl)sulfonyl]-3,4-dihydro-2H-1,2-benzothiazine 1,1-dioxide × 2 GOL GLYCEROL × 2 SO4 SULFATE ION × 7 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.5；279 K；20 % PEG 4000, 0.3 M Lithium sulfate, 0.1 M Phosphate-citrate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.10 Å R-free 0.228
3H6W Crystal structure of the iGluR2 ligand-binding core (S1S2J-N754S) in complex with glutamate and NS5217 at 1.50 A resolution Deposited 2009-04-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain A 653–796（144 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796	Mutation：N754S Mutation：N754S	GLU GLUTAMIC ACID × 2 NS7 (3R)-3-cyclopentyl-6-methyl-7-[(4-methylpiperazin-1-yl)sulfonyl]-3,4-dihydro-2H-1,2-benzothiazine 1,1-dioxide × 2 SO4 SULFATE ION × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；20 % PEG 4000, 0.1 M Ammonium sulfate, 0.1 M Cacodylate pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.49 Å R-free 0.232
3H6W Crystal structure of the iGluR2 ligand-binding core (S1S2J-N754S) in complex with glutamate and NS5217 at 1.50 A resolution Deposited 2009-04-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796 Chain B 653–796（144 aa） Fragment：iGluR2-flop ligand-binding core: UNP residues 413-796	Mutation：N754S Mutation：N754S	GLU GLUTAMIC ACID × 2 NS7 (3R)-3-cyclopentyl-6-methyl-7-[(4-methylpiperazin-1-yl)sulfonyl]-3,4-dihydro-2H-1,2-benzothiazine 1,1-dioxide × 2 SO4 SULFATE ION × 2 DMS DIMETHYL SULFOXIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；20 % PEG 4000, 0.1 M Ammonium sulfate, 0.1 M Cacodylate pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.49 Å R-free 0.232
3HSY High resolution structure of a dimeric GluR2 N-terminal domain (NTD) Deposited 2009-06-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 25–400（376 aa） Fragment：N-terminal Domain, UNP residues 25-400 Chain B 25–400（376 aa） Fragment：N-terminal Domain, UNP residues 25-400	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.8；293 K；200mM ammonium phosphatre, 20% PEG3350, pH4.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.75 Å R-free 0.205
3IJO Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, althiazide Deposited 2009-08-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Chain B 653–794（142 aa） Chain E 414–527（114 aa） Chain E 653–794（142 aa）	Not recorded	GLU GLUTAMIC ACID × 2 B4D (3S)-6-chloro-3-[(prop-2-en-1-ylsulfanyl)methyl]-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide × 2 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.00 Å R-free 0.234
3IJO Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, althiazide Deposited 2009-08-04	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain H 414–527（114 aa） Chain H 653–794（142 aa）	Not recorded	GLU GLUTAMIC ACID × 2 B4D (3S)-6-chloro-3-[(prop-2-en-1-ylsulfanyl)methyl]-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.00 Å R-free 0.234
3IJX Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, hydrochlorothiazide Deposited 2009-08-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Chain B 653–794（142 aa） Chain D 414–527（114 aa） Chain D 653–794（142 aa）	Not recorded	GLU GLUTAMIC ACID × 2 HCZ 6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.88 Å R-free 0.257
3IJX Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, hydrochlorothiazide Deposited 2009-08-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain H 414–527（114 aa） Chain H 653–794（142 aa）	Not recorded	GLU GLUTAMIC ACID × 2 HCZ 6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide × 2 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.88 Å R-free 0.257
3IK6 Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, chlorothiazide Deposited 2009-08-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain B 414–527（114 aa） Fragment：S1S2 binding domain Chain B 653–794（142 aa） Fragment：S1S2 binding domain Chain E 414–527（114 aa） Fragment：S1S2 binding domain Chain E 653–794（142 aa） Fragment：S1S2 binding domain Chain H 414–527（114 aa） Fragment：S1S2 binding domain Chain H 653–794（142 aa） Fragment：S1S2 binding domain	Not recorded	GLU GLUTAMIC ACID × 3 HCZ 6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide × 3 ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.10 Å R-free 0.245
3IL1 Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, IDRA-21 Deposited 2009-08-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：S1S2 binding domain Chain B 653–794（142 aa） Fragment：S1S2 binding domain Chain E 414–527（114 aa） Fragment：S1S2 binding domain Chain E 653–794（142 aa） Fragment：S1S2 binding domain	Mutation：N242S Mutation：N242S Mutation：N242S Mutation：N242S	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 3 B5D (3S)-7-chloro-3-methyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.00 Å R-free 0.234
3IL1 Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, IDRA-21 Deposited 2009-08-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain H 414–527（114 aa） Fragment：S1S2 binding domain Chain H 653–794（142 aa） Fragment：S1S2 binding domain	Mutation：N242S Mutation：N242S	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 4 B5D (3S)-7-chloro-3-methyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.00 Å R-free 0.234
3ILT Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, trichlormethiazide Deposited 2009-08-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain B 414–527（114 aa） Fragment：S1S2 binding domain Chain B 653–794（142 aa） Fragment：S1S2 binding domain Chain E 414–527（114 aa） Fragment：S1S2 binding domain Chain E 653–794（142 aa） Fragment：S1S2 binding domain Chain H 414–527（114 aa） Fragment：S1S2 binding domain Chain H 653–794（142 aa） Fragment：S1S2 binding domain	Mutation：N242S Mutation：N242S Mutation：N242S Mutation：N242S Mutation：N242S Mutation：N242S	GLU GLUTAMIC ACID × 3 ZN ZINC ION × 5 TRU 6-CHLORO-3-(DICHLOROMETHYL)-3,4-DIHYDRO-2H-1,2,4-BENZOTHIADIAZINE-7-SULFONAMIDE 1,1-DIOXIDE × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.11 Å R-free 0.261
3ILU Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, hydroflumethiazide Deposited 2009-08-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：S1S2 binding domain Chain B 653–794（142 aa） Fragment：S1S2 binding domain Chain E 414–527（114 aa） Fragment：S1S2 binding domain Chain E 653–794（142 aa） Fragment：S1S2 binding domain	Mutation：N242S Mutation：N242S Mutation：N242S Mutation：N242S	GLU GLUTAMIC ACID × 2 HFZ 6-(trifluoromethyl)-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.00 Å R-free 0.226
3ILU Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, hydroflumethiazide Deposited 2009-08-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain H 414–527（114 aa） Fragment：S1S2 binding domain Chain H 653–794（142 aa） Fragment：S1S2 binding domain	Mutation：N242S Mutation：N242S	GLU GLUTAMIC ACID × 2 HFZ 6-(trifluoromethyl)-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K	Resolution 2.00 Å R-free 0.226
3KG2 AMPA subtype ionotropic glutamate receptor in complex with competitive antagonist ZK 200775 Deposited 2009-10-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Fragment：sequence database residues 25-847 Chain B 25–847（823 aa） Fragment：sequence database residues 25-847 Chain C 25–847（823 aa） Fragment：sequence database residues 25-847 Chain D 25–847（823 aa） Fragment：sequence database residues 25-847	Mutation：N241E, N385D, N392Q, K410A, E413A, M414A, E416A, and C589A Mutation：N241E, N385D, N392Q, K410A, E413A, M414A, E416A, and C589A Mutation：N241E, N385D, N392Q, K410A, E413A, M414A, E416A, and C589A Mutation：N241E, N385D, N392Q, K410A, E413A, M414A, E416A, and C589A	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	X-RAY DIFFRACTION X-ray crystallization conditions 277 K；Under paraffin oil, temperature 277K	Resolution 3.60 Å R-free 0.296
3KGC Isolated ligand binding domain dimer of GluA2 ionotropic glutamate receptor in complex with glutamate, LY 404187 and ZK 200775 Deposited 2009-10-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 414–527（114 aa） Fragment：extracellular domains residues 414-527 and 653-795 Chain A 654–795（142 aa） Fragment：extracellular domains residues 414-527 and 653-795 Chain B 414–527（114 aa） Fragment：extracellular domains residues 414-527 and 653-795 Chain B 654–795（142 aa） Fragment：extracellular domains residues 414-527 and 653-795	Not recorded	GLU GLUTAMIC ACID × 1 SO4 SULFATE ION × 2 LY7 N-[(2S)-2-(4'-cyanobiphenyl-4-yl)propyl]propane-2-sulfonamide × 1 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；19% PEG 4000, 0.3 M ammonium sulfate, 0.1 M sodium acetate, pH 5.0, vapor diffusion, hanging drop, temperature 277K	Resolution 1.55 Å R-free 0.224
3LSF Piracetam bound to the ligand binding domain of GluA2 Deposited 2010-02-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Chain B 653–794（142 aa） Chain E 414–527（114 aa） Chain E 653–794（142 aa）	Mutation：N242S Mutation：N242S Mutation：N242S Mutation：N242S	GLU GLUTAMIC ACID × 2 PZI 2-(2-oxopyrrolidin-1-yl)acetamide × 4 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18% PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 M zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.85 Å R-free 0.228
3LSF Piracetam bound to the ligand binding domain of GluA2 Deposited 2010-02-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain H 414–527（114 aa） Chain H 653–794（142 aa）	Mutation：N242S Mutation：N242S	GLU GLUTAMIC ACID × 2 PZI 2-(2-oxopyrrolidin-1-yl)acetamide × 4 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18% PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 M zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.85 Å R-free 0.228
3LSL Piracetam bound to the ligand binding domain of GluA2 (flop form) Deposited 2010-02-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 414–527（114 aa） Chain A 653–794（142 aa） Chain D 414–527（114 aa） Chain D 653–794（142 aa）	Not recorded	GLU GLUTAMIC ACID × 2 PZI 2-(2-oxopyrrolidin-1-yl)acetamide × 6 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18% PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 M zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.12 Å R-free 0.263
3LSL Piracetam bound to the ligand binding domain of GluA2 (flop form) Deposited 2010-02-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 414–527（114 aa） Chain G 653–794（142 aa）	Not recorded	GLU GLUTAMIC ACID × 2 PZI 2-(2-oxopyrrolidin-1-yl)acetamide × 6 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18% PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 M zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.12 Å R-free 0.263
3M3L PEPA bound to the ligand binding domain of GluA2 (flop form) Deposited 2010-03-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain A 653–794（142 aa） Fragment：UNP residues 414-527, 652-794 Chain D 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain D 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	GLU GLUTAMIC ACID × 2 P99 2-[2,6-difluoro-4-({2-[(phenylsulfonyl)amino]ethyl}sulfanyl)phenoxy]acetamide × 1 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG 8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.85 Å R-free 0.242
3M3L PEPA bound to the ligand binding domain of GluA2 (flop form) Deposited 2010-03-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 414–527（114 aa） Fragment：UNP residues 414-527, 652-794 Chain G 653–794（142 aa） Fragment：UNP residues 414-527, 652-794	Not recorded	GLU GLUTAMIC ACID × 2 P99 2-[2,6-difluoro-4-({2-[(phenylsulfonyl)amino]ethyl}sulfanyl)phenoxy]acetamide × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG 8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.85 Å R-free 0.242
3N6V Structure of the GluA2 NTD-dimer interface mutant, T78A Deposited 2010-05-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 27–400（374 aa） Fragment：N-terminal domain Chain B 27–400（374 aa） Fragment：N-terminal domain	Mutation：T78A Mutation：T78A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；100mM Tris, 200mM MgCl2, 20% PEG 8000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 3.20 Å R-free 0.265
3N6V Structure of the GluA2 NTD-dimer interface mutant, T78A Deposited 2010-05-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 27–400（374 aa） Fragment：N-terminal domain Chain D 27–400（374 aa） Fragment：N-terminal domain	Mutation：T78A Mutation：T78A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；100mM Tris, 200mM MgCl2, 20% PEG 8000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 3.20 Å R-free 0.265
3N6V Structure of the GluA2 NTD-dimer interface mutant, T78A Deposited 2010-05-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 27–400（374 aa） Fragment：N-terminal domain Chain F 27–400（374 aa） Fragment：N-terminal domain	Mutation：T78A Mutation：T78A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；100mM Tris, 200mM MgCl2, 20% PEG 8000, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 3.20 Å R-free 0.265
3O28 Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2010-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796 Chain A 653–795（143 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796	Not recorded	O28 2-({[3-(trifluoromethyl)-4,5,6,7-tetrahydro-1H-indazol-1-yl]acetyl}amino)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide × 2 GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 6 DMS DIMETHYL SULFOXIDE × 2 GOL GLYCEROL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；16% PEG 8000, 100mM Sodium Cacodylate pH 4.5, 50mM Lithium Sulphate, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.234
3O29 Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2010-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796 Chain A 653–795（143 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796	Not recorded	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 8 O29 N-[2-(dimethylamino)ethyl]-2-({[3-(trifluoromethyl)-4,5,6,7-tetrahydro-1H-indazol-1-yl]acetyl}amino)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；12% PEG 4000, 100mM Sodium Cacodylate pH 4.5, 50mM Lithium Sulphate, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.02 Å R-free 0.250
3O2A Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2010-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796 Chain A 653–795（143 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796	Not recorded	O30 N-(3-aminopropyl)-2-({[3-(trifluoromethyl)-4,5,6,7-tetrahydro-1H-indazol-1-yl]acetyl}amino)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide × 2 GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；18% PEG 4000, 100mM Sodium Cacodylate pH 4.5, 50mM Lithium Sulphate, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.217
3O2J Structure of the GluA2 NTD-dimer interface mutant, N54A Deposited 2010-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 22–400（379 aa） Fragment：N-terminal domain Chain B 22–400（379 aa） Fragment：N-terminal domain	Mutation：N54A Mutation：N54A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；291 K；18% PEG 3350, 100mM sodium citrate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 1.95 Å R-free 0.247
3O6G Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2010-07-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796 Chain A 653–795（143 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796	Not recorded	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 6 O27 N-[(3R)-pyrrolidin-3-yl]-2-({[3-(trifluoromethyl)-4,5,6,7-tetrahydro-1H-indazol-1-yl]acetyl}amino)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide × 2 EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；17% PEG 4000, 100mM Sodium Cacodylate pH 4.0, 50mM Lithium Sulphate, 2.5% Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.223
3O6H Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2010-07-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796 Chain A 653–795（143 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796	Not recorded	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 6 O25 2-[({4-[(ethylamino)methyl]-3-(trifluoromethyl)-1H-pyrazol-1-yl}acetyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide × 2 DMS DIMETHYL SULFOXIDE × 2 EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；18% PEG 4000, 100mM Sodium Cacodylate pH 4.0, 50mM Lithium Sulphate, 5% Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.10 Å R-free 0.263
3O6I Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2010-07-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796 Chain A 653–795（143 aa） Fragment：Ligand binding domain, UNP residues 413 to 527 and 653 to 796	Not recorded	GLU GLUTAMIC ACID × 2 O26 2-[({3-tert-butyl-4-[(methylamino)methyl]-1H-pyrazol-1-yl}acetyl)amino]-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide × 2 SO4 SULFATE ION × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.3；277 K；18% PEG 4000, 50mM Lithium sulphate, 2.5% Glycerol, 100mM Sodium Cacodylate pH 4.3, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.247
3PD8 X-ray structure of the ligand-binding core of GluA2 in complex with (S)-7-HPCA at 2.5 A resolution Deposited 2010-10-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：UNP residues 413-527, 653-795 Chain A 653–795（143 aa） Fragment：UNP residues 413-527, 653-795 Chain B 413–527（115 aa） Fragment：UNP residues 413-527, 653-795 Chain B 653–795（143 aa） Fragment：UNP residues 413-527, 653-795	Not recorded	ZN ZINC ION × 3 HA7 (7S)-3-hydroxy-4,5,6,7-tetrahydroisoxazolo[5,4-c]pyridine-7-carboxylic acid × 2 GOL GLYCEROL × 1 ACY ACETIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；280 K；PEG4000, zinc acetate, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.48 Å R-free 0.261
3PD8 X-ray structure of the ligand-binding core of GluA2 in complex with (S)-7-HPCA at 2.5 A resolution Deposited 2010-10-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Fragment：UNP residues 413-527, 653-795 Chain C 653–795（143 aa） Fragment：UNP residues 413-527, 653-795	Not recorded	ZN ZINC ION × 4 HA7 (7S)-3-hydroxy-4,5,6,7-tetrahydroisoxazolo[5,4-c]pyridine-7-carboxylic acid × 2 CAC CACODYLATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；280 K；PEG4000, zinc acetate, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.48 Å R-free 0.261
3PD9 X-ray structure of the ligand-binding core of GluA2 in complex with (R)-5-HPCA at 2.1 A resolution Deposited 2010-10-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：UNP residues 413-527, 653-795 Chain A 653–795（143 aa） Fragment：UNP residues 413-527, 653-795 Chain B 413–527（115 aa） Fragment：UNP residues 413-527, 653-795 Chain B 653–795（143 aa） Fragment：UNP residues 413-527, 653-795	Not recorded	HA5 (5R)-3-hydroxy-4,5,6,7-tetrahydroisoxazolo[5,4-c]pyridine-5-carboxylic acid × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 5 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；PEG4000, ammonium sulfate, acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.10 Å R-free 0.233
3PMV Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2010-11-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, residues 413 to 527 and 653 to 796 Chain A 653–796（144 aa） Fragment：Ligand binding domain, residues 413 to 527 and 653 to 796	Not recorded	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 10 557 N-[(2S)-2-{4-[4-(hydroxymethyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]phenyl}propyl]propane-2-sulfonamide × 2 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；18% PEG 4000, 50mM Lithium Sulphate, 2.5% Glycerol, 100mM Sodium Cacodylate pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.252
3PMW Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2010-11-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, residues 413 to 527 and 653 to 796 Chain A 653–796（144 aa） Fragment：Ligand binding domain, residues 413 to 527 and 653 to 796	Mutation：S1-S2 fusion in which Gly118 and Thr119 replace a membrane-spanning region Mutation：S1-S2 fusion in which Gly118 and Thr119 replace a membrane-spanning region	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 14 GOL GLYCEROL × 4 DMS DIMETHYL SULFOXIDE × 2 G69 N-[(2S)-5-{[4-(hydroxymethyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]methyl}-2,3-dihydro-1H-inden-2-yl]propane-2-sulfonami de × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；18% PEG 4000, 50mM Lithium Sulphate, 2.5% Glycerol, 100mM Sodium Cacodylate pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.313
3PMX Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2010-11-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, residues 413 to 527 and 653 to 796 Chain A 653–796（144 aa） Fragment：Ligand binding domain, residues 413 to 527 and 653 to 796	Not recorded	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 8 GOL GLYCEROL × 4 DMS DIMETHYL SULFOXIDE × 4 EDO 1,2-ETHANEDIOL × 8 808 N-[(2S)-5-{[5-(trifluoromethyl)furan-2-yl]methyl}-2,3-dihydro-1H-inden-2-yl]propane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；18% PEG 4000, 50mM Lithium Sulphate, 2.5% Glycerol, 100mM Sodium Cacodylate pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.87 Å R-free 0.281
3RTF Chlorowillardiine bound to the ligand binding domain of GluA2 Deposited 2011-05-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：SEE REMARK 999 Chain B 653–794（142 aa） Fragment：SEE REMARK 999 Chain D 414–527（114 aa） Fragment：SEE REMARK 999 Chain D 653–794（142 aa） Fragment：SEE REMARK 999	Not recorded	CWD 3-(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-L-alanine × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.203
3RTF Chlorowillardiine bound to the ligand binding domain of GluA2 Deposited 2011-05-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain F 414–527（114 aa） Fragment：SEE REMARK 999 Chain F 653–794（142 aa） Fragment：SEE REMARK 999	Not recorded	CWD 3-(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-L-alanine × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.203
3RTW Nitrowillardiine bound to the ligand binding domain of GluA2 Deposited 2011-05-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：SEE REMARK 999 Chain B 653–794（142 aa） Fragment：SEE REMARK 999 Chain D 414–527（114 aa） Fragment：SEE REMARK 999 Chain D 653–794（142 aa） Fragment：SEE REMARK 999	Not recorded	NWD 3-(5-nitro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-L-alanine × 2 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.10 Å R-free 0.259
3RTW Nitrowillardiine bound to the ligand binding domain of GluA2 Deposited 2011-05-04	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain F 414–527（114 aa） Fragment：SEE REMARK 999 Chain F 653–794（142 aa） Fragment：SEE REMARK 999	Not recorded	NWD 3-(5-nitro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-L-alanine × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.10 Å R-free 0.259
3T93 Glutamate bound to a double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2 Deposited 2011-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：SEE REMARK 999 Chain B 653–794（142 aa） Fragment：SEE REMARK 999 Chain D 414–527（114 aa） Fragment：SEE REMARK 999 Chain D 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.91 Å R-free 0.229
3T93 Glutamate bound to a double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2 Deposited 2011-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain F 414–527（114 aa） Fragment：SEE REMARK 999 Chain F 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：A473C/S673C Mutation：A473C/S673C	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.91 Å R-free 0.229
3T96 Iodowillardiine bound to a double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2 Deposited 2011-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：SEE REMARK 999 Chain B 653–794（142 aa） Fragment：SEE REMARK 999 Chain D 414–527（114 aa） Fragment：SEE REMARK 999 Chain D 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C	IWD 2-AMINO-3-(5-IODO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.87 Å R-free 0.219
3T96 Iodowillardiine bound to a double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2 Deposited 2011-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain F 414–527（114 aa） Fragment：SEE REMARK 999 Chain F 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：A473C/S673C Mutation：A473C/S673C	IWD 2-AMINO-3-(5-IODO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.87 Å R-free 0.219
3T9H Kainate bound to a double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2 Deposited 2011-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：SEE REMARK 999 Chain B 653–794（142 aa） Fragment：SEE REMARK 999 Chain D 414–527（114 aa） Fragment：SEE REMARK 999 Chain D 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.02 Å R-free 0.235
3T9H Kainate bound to a double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2 Deposited 2011-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain F 414–527（114 aa） Fragment：SEE REMARK 999 Chain F 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：A473C/S673C Mutation：A473C/S673C	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.02 Å R-free 0.235
3T9U CNQX bound to an oxidized double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2 Deposited 2011-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 414–527（114 aa） Fragment：SEE REMARK 999 Chain A 653–794（142 aa） Fragment：SEE REMARK 999 Chain B 414–527（114 aa） Fragment：SEE REMARK 999 Chain B 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C	CNI 7-nitro-2,3-dioxo-2,3-dihydroquinoxaline-6-carbonitrile × 2 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.97 Å R-free 0.219
3T9U CNQX bound to an oxidized double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2 Deposited 2011-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 414–527（114 aa） Fragment：SEE REMARK 999 Chain C 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：A473C/S673C Mutation：A473C/S673C	CNI 7-nitro-2,3-dioxo-2,3-dihydroquinoxaline-6-carbonitrile × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.97 Å R-free 0.219
3T9V CNQX bound to a reduced double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2 Deposited 2011-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 414–527（114 aa） Fragment：SEE REMARK 999 Chain A 653–794（142 aa） Fragment：SEE REMARK 999 Chain B 414–527（114 aa） Fragment：SEE REMARK 999 Chain B 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C Mutation：A473C/S673C	CNI 7-nitro-2,3-dioxo-2,3-dihydroquinoxaline-6-carbonitrile × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.98 Å R-free 0.238
3T9X Glutamate bound to a double cysteine mutant (V484C/E657C) of the ligand binding domain of GluA2 Deposited 2011-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：SEE REMARK 999 Chain B 653–794（142 aa） Fragment：SEE REMARK 999 Chain F 414–527（114 aa） Fragment：SEE REMARK 999 Chain F 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：V505C/E678C Mutation：V505C/E678C Mutation：V505C/E678C Mutation：V505C/E678C	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.82 Å R-free 0.240
3T9X Glutamate bound to a double cysteine mutant (V484C/E657C) of the ligand binding domain of GluA2 Deposited 2011-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 414–527（114 aa） Fragment：SEE REMARK 999 Chain D 653–794（142 aa） Fragment：SEE REMARK 999	Mutation：V505C/E678C Mutation：V505C/E678C	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.82 Å R-free 0.240
3TDJ Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and BPAM-97 at 1.95 A resolution Deposited 2011-08-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP residues 413-527 and 653-796 Chain A 653–796（144 aa） Fragment：Ligand binding domain, UNP residues 413-527 and 653-796 Chain B 413–527（115 aa） Fragment：Ligand binding domain, UNP residues 413-527 and 653-796 Chain B 653–796（144 aa） Fragment：Ligand binding domain, UNP residues 413-527 and 653-796	Mutation：L483Y, N754S Mutation：L483Y, N754S Mutation：L483Y, N754S Mutation：L483Y, N754S	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 3 CL CHLORIDE ION × 5 GOL GLYCEROL × 11 3TJ 4-ethyl-7-fluoro-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；15.2% PEG4000, 0.3 M lithium sulfate and 0.1 M phosphate-citrate., pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.95 Å R-free 0.215
3TKD Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and cyclothiazide at 1.45 A resolution Deposited 2011-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain Chain A 653–795（143 aa） Fragment：Ligand binding domain Chain B 413–527（115 aa） Fragment：Ligand binding domain Chain B 653–795（143 aa） Fragment：Ligand binding domain	Mutation：L483Y, N754S Mutation：L483Y, N754S Mutation：L483Y, N754S Mutation：L483Y, N754S	GLU GLUTAMIC ACID × 2 CYZ CYCLOTHIAZIDE × 2 SO4 SULFATE ION × 8 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；20% PEG4000, 0.3M ammonium sulfate, 0.1M phosphate-citrate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.45 Å R-free 0.180
3TZA Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (S)-2-amino-3-(2-(2-carboxyethyl)-5-chloro-4-nitrophenyl)propionic acid at 1.9A resolution Deposited 2011-09-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP resiudes 413-527,UNP residues 653-796 Chain A 653–796（144 aa） Fragment：Ligand binding domain, UNP resiudes 413-527,UNP residues 653-796 Chain B 413–527（115 aa） Fragment：Ligand binding domain, UNP resiudes 413-527,UNP residues 653-796 Chain B 653–796（144 aa） Fragment：Ligand binding domain, UNP resiudes 413-527,UNP residues 653-796	Not recorded	TZG (S)-2-amino-3-(2-(2-carboxyethyl)-5-chloro-4-nitrophenyl)propionic acid × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；15.2% PEG4000, 0.1M ammonium sulfate, 0.1M sodium acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.90 Å R-free 0.230
4FAT Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator Deposited 2012-05-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：ligand binding domain Chain A 653–796（144 aa） Fragment：ligand binding domain	Mutation：delta 528-652 Mutation：delta 528-652	GLU GLUTAMIC ACID × 2 496 2-({[4-(hydroxymethyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]acetyl}amino)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide × 2 SO4 SULFATE ION × 6 GOL GLYCEROL × 8 LI LITHIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.1；298 K；18% PEG 4000, 50mM Lithium Sulphate, 100mM Sodium Cacodylate, pH 4.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.40 Å R-free 0.209
4G8M Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the agonist CBG-IV at 2.05A resolution Deposited 2012-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：UNP residues 413-527, 653-796 Chain A 653–796（144 aa） Fragment：UNP residues 413-527, 653-796 Chain B 413–527（115 aa） Fragment：UNP residues 413-527, 653-796 Chain B 653–796（144 aa） Fragment：UNP residues 413-527, 653-796	Not recorded	G8M (1S,2R)-2-[(S)-amino(carboxy)methyl]cyclobutanecarboxylic acid × 2 SO4 SULFATE ION × 7 CL CHLORIDE ION × 3 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；24.4% PEG4000, 0.3M lithium sulfate, 0.1M phosphate-citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.05 Å R-free 0.228
4G8M Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the agonist CBG-IV at 2.05A resolution Deposited 2012-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：UNP residues 413-527, 653-796 Chain A 653–796（144 aa） Fragment：UNP residues 413-527, 653-796 Chain B 413–527（115 aa） Fragment：UNP residues 413-527, 653-796 Chain B 653–796（144 aa） Fragment：UNP residues 413-527, 653-796	Not recorded	G8M (1S,2R)-2-[(S)-amino(carboxy)methyl]cyclobutanecarboxylic acid × 2 SO4 SULFATE ION × 7 CL CHLORIDE ION × 3 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；24.4% PEG4000, 0.3M lithium sulfate, 0.1M phosphate-citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.05 Å R-free 0.228
4GXS Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin Deposited 2012-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Fragment：UNP Residues 652-794 Chain B 653–794（142 aa） Fragment：UNP Residues 652-794 Chain D 414–527（114 aa） Fragment：UNP Residues 652-794 Chain D 653–794（142 aa） Fragment：UNP Residues 652-794	Not recorded	0YS (5R)-2-[(1S,2R)-2-amino-2-carboxy-1-hydroxyethyl]-5-{(2S)-2-carboxy-2-[(3,5-dichloro-4-hydroxybenzoyl)amino]ethyl}-L-proline × 2 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16-18% PEG 8K, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.96 Å R-free 0.225
4H8J Structure of GluA2-LBD in complex with MES Deposited 2012-09-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：SEE REMARK 999 Chain A 653–797（145 aa） Fragment：SEE REMARK 999 Chain B 413–527（115 aa） Fragment：SEE REMARK 999 Chain B 653–797（145 aa） Fragment：SEE REMARK 999	Not recorded	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 SO4 SULFATE ION × 6 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；23-27% w/v PEG3350, 0.2 M lithium sulfate, MES sodium, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.221
4H8J Structure of GluA2-LBD in complex with MES Deposited 2012-09-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Fragment：SEE REMARK 999 Chain C 653–797（145 aa） Fragment：SEE REMARK 999 Chain D 413–527（115 aa） Fragment：SEE REMARK 999 Chain D 653–797（145 aa） Fragment：SEE REMARK 999	Not recorded	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 SO4 SULFATE ION × 6 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；23-27% w/v PEG3350, 0.2 M lithium sulfate, MES sodium, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.221
4IGT Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the agonist ZA302 at 1.24A resolution Deposited 2012-12-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand-binding domain, UNP RESIDUES 413-527, 653-796 Chain A 653–796（144 aa） Fragment：Ligand-binding domain, UNP RESIDUES 413-527, 653-796	Not recorded	3ZA (4R)-4-{3-[hydroxy(methyl)amino]-3-oxopropyl}-L-glutamic acid × 2 SO4 SULFATE ION × 6 LI LITHIUM ION × 2 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；15.2% PEG 4000, 0.1M Li2SO4, 0.1M phosphate-citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 1.24 Å R-free 0.155
4ISU Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (2R)-IKM-159 at 2.3A resolution. Deposited 2013-01-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand-binding domain Chain A 653–796（144 aa） Fragment：Ligand-binding domain Chain C 413–527（115 aa） Fragment：Ligand-binding domain Chain C 653–796（144 aa） Fragment：Ligand-binding domain	Not recorded	IKM (4aS,5aR,6R,8aS,8bS)-5a-(carboxymethyl)-8-oxo-2,4a,5a,6,7,8,8a,8b-octahydro-1H-pyrrolo[3',4':4,5]furo[3,2-b]pyridine-6-carboxylic acid × 1 SO4 SULFATE ION × 3 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；20% PEG4000, 0.1M Lithium sulfate, 0.1M phosphate-citrate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.30 Å R-free 0.258
4ISU Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (2R)-IKM-159 at 2.3A resolution. Deposited 2013-01-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：Ligand-binding domain Chain B 653–796（144 aa） Fragment：Ligand-binding domain Chain D 413–527（115 aa） Fragment：Ligand-binding domain Chain D 653–796（144 aa） Fragment：Ligand-binding domain	Not recorded	IKM (4aS,5aR,6R,8aS,8bS)-5a-(carboxymethyl)-8-oxo-2,4a,5a,6,7,8,8a,8b-octahydro-1H-pyrrolo[3',4':4,5]furo[3,2-b]pyridine-6-carboxylic acid × 1 SO4 SULFATE ION × 3 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；20% PEG4000, 0.1M Lithium sulfate, 0.1M phosphate-citrate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.30 Å R-free 0.258
4ISU Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (2R)-IKM-159 at 2.3A resolution. Deposited 2013-01-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Fragment：Ligand-binding domain Chain A 653–796（144 aa） Fragment：Ligand-binding domain	Not recorded	IKM (4aS,5aR,6R,8aS,8bS)-5a-(carboxymethyl)-8-oxo-2,4a,5a,6,7,8,8a,8b-octahydro-1H-pyrrolo[3',4':4,5]furo[3,2-b]pyridine-6-carboxylic acid × 1 SO4 SULFATE ION × 1 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；20% PEG4000, 0.1M Lithium sulfate, 0.1M phosphate-citrate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.30 Å R-free 0.258
4ISU Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (2R)-IKM-159 at 2.3A resolution. Deposited 2013-01-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 413–527（115 aa） Fragment：Ligand-binding domain Chain D 653–796（144 aa） Fragment：Ligand-binding domain	Not recorded	SO4 SULFATE ION × 1 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；20% PEG4000, 0.1M Lithium sulfate, 0.1M phosphate-citrate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.30 Å R-free 0.258
4ISU Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (2R)-IKM-159 at 2.3A resolution. Deposited 2013-01-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 413–527（115 aa） Fragment：Ligand-binding domain Chain C 653–796（144 aa） Fragment：Ligand-binding domain	Not recorded	SO4 SULFATE ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；20% PEG4000, 0.1M Lithium sulfate, 0.1M phosphate-citrate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.30 Å R-free 0.258
4ISU Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (2R)-IKM-159 at 2.3A resolution. Deposited 2013-01-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：Ligand-binding domain Chain B 653–796（144 aa） Fragment：Ligand-binding domain	Not recorded	IKM (4aS,5aR,6R,8aS,8bS)-5a-(carboxymethyl)-8-oxo-2,4a,5a,6,7,8,8a,8b-octahydro-1H-pyrrolo[3',4':4,5]furo[3,2-b]pyridine-6-carboxylic acid × 1 SO4 SULFATE ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；20% PEG4000, 0.1M Lithium sulfate, 0.1M phosphate-citrate pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 2.30 Å R-free 0.258
4IY5 Crystal structure of the glua2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and CX516 at 2.0 A resolution Deposited 2013-01-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP RESIDUES 413-527, 653-796 Chain A 653–796（144 aa） Fragment：Ligand binding domain, UNP RESIDUES 413-527, 653-796 Chain B 413–527（115 aa） Fragment：Ligand binding domain, UNP RESIDUES 413-527, 653-796 Chain B 653–796（144 aa） Fragment：Ligand binding domain, UNP RESIDUES 413-527, 653-796	Mutation：L94Y, N242S Mutation：L94Y, N242S Mutation：L94Y, N242S Mutation：L94Y, N242S	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 5 GOL GLYCEROL × 3 CL CHLORIDE ION × 3 CX5 piperidin-1-yl(quinoxalin-6-yl)methanone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；24.4% PEG 4000, 0.3M lithium sulfate, 0.1M phosphate-citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 2.00 Å R-free 0.200
4IY6 Crystal structure of the GLUA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and ME-CX516 at 1.72 A resolution Deposited 2013-01-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, UNP RESIDUES 413-527, 653-796 Chain A 653–796（144 aa） Fragment：Ligand binding domain, UNP RESIDUES 413-527, 653-796	Mutation：L94Y, N242S Mutation：L94Y, N242S	MQR [(3R)-3-methylpiperidin-1-yl](quinoxalin-6-yl)methanone × 2 MQS [(3S)-3-methylpiperidin-1-yl](quinoxalin-6-yl)methanone × 4 GLU GLUTAMIC ACID × 2 GOL GLYCEROL × 2 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；15.2% PEG 4000, 0.3M lithium sulfate, 0.1M sodium acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.72 Å R-free 0.168
4L17 GluA2-L483Y-A665C ligand-binding domain in complex with the antagonist DNQX Deposited 2013-06-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain (UNP residues 413-527, 653-796) Chain A 653–796（144 aa） Fragment：Ligand binding domain (UNP residues 413-527, 653-796) Chain C 413–527（115 aa） Fragment：Ligand binding domain (UNP residues 413-527, 653-796) Chain C 653–796（144 aa） Fragment：Ligand binding domain (UNP residues 413-527, 653-796)	Mutation：L94Y, A153C Mutation：L94Y, A153C Mutation：L94Y, A153C Mutation：L94Y, A153C	DNQ 6,7-DINITROQUINOXALINE-2,3-DIONE × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277.15 K；19% PEG 1450, 0.3M lithium sulfate, 0.1M cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K	Resolution 2.80 Å R-free 0.244
4L17 GluA2-L483Y-A665C ligand-binding domain in complex with the antagonist DNQX Deposited 2013-06-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 413–527（115 aa） Fragment：Ligand binding domain (UNP residues 413-527, 653-796) Chain E 653–796（144 aa） Fragment：Ligand binding domain (UNP residues 413-527, 653-796)	Mutation：L94Y, A153C Mutation：L94Y, A153C	DNQ 6,7-DINITROQUINOXALINE-2,3-DIONE × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277.15 K；19% PEG 1450, 0.3M lithium sulfate, 0.1M cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K	Resolution 2.80 Å R-free 0.244
4L17 GluA2-L483Y-A665C ligand-binding domain in complex with the antagonist DNQX Deposited 2013-06-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 413–527（115 aa） Fragment：Ligand binding domain (UNP residues 413-527, 653-796) Chain G 653–796（144 aa） Fragment：Ligand binding domain (UNP residues 413-527, 653-796)	Mutation：L94Y, A153C Mutation：L94Y, A153C	DNQ 6,7-DINITROQUINOXALINE-2,3-DIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277.15 K；19% PEG 1450, 0.3M lithium sulfate, 0.1M cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K	Resolution 2.80 Å R-free 0.244
4LZ5 Crystal structures of GLuR2 ligand-binding-domain in complex with glutamate and positive allosteric modulators Deposited 2013-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 404–527（124 aa） Fragment：SEE REMARK 999 Chain A 653–796（144 aa） Fragment：SEE REMARK 999 Chain C 404–527（124 aa） Fragment：SEE REMARK 999 Chain C 653–796（144 aa） Fragment：SEE REMARK 999	Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 2 1YV N-[(2R)-2-(4'-cyanobiphenyl-4-yl)propyl]propane-2-sulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1 uL 7 mg/mL protein in 10 mM (S)-Glu, 10 mM HEPES, pH 7.5, 20 mM sodium chloride, 1 mM EDTA, 150 uM ligand (from 30 mM DMSO stock) + 1 uL reservoir (10% PEG8000, 0.1 M zinc acetate, 0.1 M sodium acetate, pH 5.5), crystals appeared in 3-5 days, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.50 Å R-free 0.203
4LZ5 Crystal structures of GLuR2 ligand-binding-domain in complex with glutamate and positive allosteric modulators Deposited 2013-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 404–527（124 aa） Fragment：SEE REMARK 999 Chain B 653–796（144 aa） Fragment：SEE REMARK 999	Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 6 1YV N-[(2R)-2-(4'-cyanobiphenyl-4-yl)propyl]propane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1 uL 7 mg/mL protein in 10 mM (S)-Glu, 10 mM HEPES, pH 7.5, 20 mM sodium chloride, 1 mM EDTA, 150 uM ligand (from 30 mM DMSO stock) + 1 uL reservoir (10% PEG8000, 0.1 M zinc acetate, 0.1 M sodium acetate, pH 5.5), crystals appeared in 3-5 days, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.50 Å R-free 0.203
4LZ7 Crystal structures of GLuR2 ligand-binding-domain in complex with glutamate and positive allosteric modulators Deposited 2013-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 404–527（124 aa） Fragment：SEE REMARK 999 Chain A 653–796（144 aa） Fragment：SEE REMARK 999 Chain C 404–527（124 aa） Fragment：SEE REMARK 999 Chain C 653–796（144 aa） Fragment：SEE REMARK 999	Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A	ZN ZINC ION × 3 GLU GLUTAMIC ACID × 2 1YW N-({(5S)-3-[3-fluoro-4-(pyrrolidin-1-yl)phenyl]-4,5-dihydro-1,2-oxazol-5-yl}methyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1 uL 7 mg/mL protein in 10 mM (S)-Glu, 10 mM HEPES, pH 7.5, 20 mM sodium chloride, 1 mM EDTA, 150 uM ligand (from 30 mM DMSO stock) + 1 uL reservoir (10% PEG8000, 0.1 M zinc acetate, 0.1 M sodium acetate, pH 5.5), crystals appeared in 3-5 days, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.10 Å R-free 0.240
4LZ7 Crystal structures of GLuR2 ligand-binding-domain in complex with glutamate and positive allosteric modulators Deposited 2013-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 404–527（124 aa） Fragment：SEE REMARK 999 Chain B 653–796（144 aa） Fragment：SEE REMARK 999	Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A	ZN ZINC ION × 4 GLU GLUTAMIC ACID × 2 1YW N-({(5S)-3-[3-fluoro-4-(pyrrolidin-1-yl)phenyl]-4,5-dihydro-1,2-oxazol-5-yl}methyl)acetamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1 uL 7 mg/mL protein in 10 mM (S)-Glu, 10 mM HEPES, pH 7.5, 20 mM sodium chloride, 1 mM EDTA, 150 uM ligand (from 30 mM DMSO stock) + 1 uL reservoir (10% PEG8000, 0.1 M zinc acetate, 0.1 M sodium acetate, pH 5.5), crystals appeared in 3-5 days, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.10 Å R-free 0.240
4LZ8 Crystal structures of GLuR2 ligand-binding-domain in complex with glutamate and positive allosteric modulators Deposited 2013-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 404–527（124 aa） Fragment：SEE REMARK 999 Chain A 653–796（144 aa） Fragment：SEE REMARK 999 Chain C 404–527（124 aa） Fragment：SEE REMARK 999 Chain C 653–796（144 aa） Fragment：SEE REMARK 999	Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A	GLU GLUTAMIC ACID × 2 1YX N-[(3S)-1-{2-fluoro-4-[(5S)-5-{[(propan-2-ylsulfonyl)amino]methyl}-4,5-dihydro-1,2-oxazol-3-yl]phenyl}pyrrolidin-3-yl]acetamide × 1 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1 uL 7 mg/mL protein in 10 mM (S)-Glu, 10 mM HEPES, pH 7.5, 20 mM sodium chloride, 1 mM EDTA, 150 uM ligand (from 30 mM DMSO stock) + 1 uL reservoir (10% PEG8000, 0.1 M zinc acetate, 0.1 M sodium acetate, pH 5.5), crystals appeared in 3-5 days, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.85 Å R-free 0.232
4LZ8 Crystal structures of GLuR2 ligand-binding-domain in complex with glutamate and positive allosteric modulators Deposited 2013-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 404–527（124 aa） Fragment：SEE REMARK 999 Chain B 653–796（144 aa） Fragment：SEE REMARK 999	Mutation：G389R,L390G,E391A Mutation：G389R,L390G,E391A	GLU GLUTAMIC ACID × 2 1YX N-[(3S)-1-{2-fluoro-4-[(5S)-5-{[(propan-2-ylsulfonyl)amino]methyl}-4,5-dihydro-1,2-oxazol-3-yl]phenyl}pyrrolidin-3-yl]acetamide × 2 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；1 uL 7 mg/mL protein in 10 mM (S)-Glu, 10 mM HEPES, pH 7.5, 20 mM sodium chloride, 1 mM EDTA, 150 uM ligand (from 30 mM DMSO stock) + 1 uL reservoir (10% PEG8000, 0.1 M zinc acetate, 0.1 M sodium acetate, pH 5.5), crystals appeared in 3-5 days, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.85 Å R-free 0.232
4N07 Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and BPAM-344 at 1.87 A resolution Deposited 2013-10-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：unp residues 413-527, unp reisdues 653-796 Chain A 653–796（144 aa） Fragment：unp residues 413-527, unp reisdues 653-796	Mutation：L504Y, N755S Mutation：L504Y, N755S	2J9 4-cyclopropyl-7-fluoro-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide × 2 GLU GLUTAMIC ACID × 2 ACT ACETATE ION × 12 ZN ZINC ION × 8 CAC CACODYLATE ION × 2 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16.5% PEG4000, 0.15 M zinc acetate, 0.1 M cacodylate, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.87 Å R-free 0.211
4N07 Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and BPAM-344 at 1.87 A resolution Deposited 2013-10-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：unp residues 413-527, unp reisdues 653-796 Chain B 653–796（144 aa） Fragment：unp residues 413-527, unp reisdues 653-796 Chain C 413–527（115 aa） Fragment：unp residues 413-527, unp reisdues 653-796 Chain C 653–796（144 aa） Fragment：unp residues 413-527, unp reisdues 653-796	Mutation：L504Y, N755S Mutation：L504Y, N755S Mutation：L504Y, N755S Mutation：L504Y, N755S	2J9 4-cyclopropyl-7-fluoro-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide × 2 GLU GLUTAMIC ACID × 2 ACT ACETATE ION × 7 ZN ZINC ION × 6 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；16.5% PEG4000, 0.15 M zinc acetate, 0.1 M cacodylate, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.87 Å R-free 0.211
4O3A Crystal structure of the glua2 ligand-binding domain in complex with L-aspartate at 1.80 a resolution Deposited 2013-12-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736) Chain A 653–796（144 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736)	Not recorded	GOL GLYCEROL × 12 ASP ASPARTIC ACID × 2 ZN ZINC ION × 6 ACT ACETATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；24.4 % PEG 4000, 0.1 M zinc acetate and 0.1 M sodium acetate., pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.80 Å R-free 0.188
4O3A Crystal structure of the glua2 ligand-binding domain in complex with L-aspartate at 1.80 a resolution Deposited 2013-12-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736) Chain B 653–796（144 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736)	Not recorded	GOL GLYCEROL × 4 ASP ASPARTIC ACID × 1 ZN ZINC ION × 2 ACT ACETATE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 3 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；24.4 % PEG 4000, 0.1 M zinc acetate and 0.1 M sodium acetate., pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.80 Å R-free 0.188
4O3A Crystal structure of the glua2 ligand-binding domain in complex with L-aspartate at 1.80 a resolution Deposited 2013-12-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 413–527（115 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736) Chain C 653–796（144 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736)	Not recorded	GOL GLYCEROL × 2 ASP ASPARTIC ACID × 1 ZN ZINC ION × 4 ACT ACETATE ION × 6 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；24.4 % PEG 4000, 0.1 M zinc acetate and 0.1 M sodium acetate., pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.80 Å R-free 0.188
4O3B Crystal structure of an open/closed glua2 ligand-binding domain dimer at 1.91 A resolution Deposited 2013-12-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736) Chain A 653–796（144 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736) Chain B 413–527（115 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736) Chain B 653–796（144 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-736)	Not recorded	SO4 SULFATE ION × 4 GOL GLYCEROL × 6 CL CHLORIDE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 ACT ACETATE ION × 1 GLU GLUTAMIC ACID × 1 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；20% PEG 4000, 0.1 M lithium sulfate and 0.1 M phosphate-citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.91 Å R-free 0.178
4O3C Crystal structure of the GLUA2 ligand-binding domain in complex with L-aspartate at 1.50 A resolution Deposited 2013-12-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-796) Chain A 653–796（144 aa） Fragment：Ligand binding domain (unp residues 413-527 and unp residues 653-796)	Not recorded	ASP ASPARTIC ACID × 2 CL CHLORIDE ION × 2 GOL GLYCEROL × 2 ACT ACETATE ION × 2 LI LITHIUM ION × 2 SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；20% PEG 4000, 0.1 M lithium sulfate and 0.1 M phosphate-citrate., pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K	Resolution 1.50 Å R-free 0.158
4Q30 Nitrowillardiine bound to the ligand binding domain of GluA2 at pH 3.5 Deposited 2014-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 414–527（114 aa） Chain B 653–794（142 aa） Chain D 414–527（114 aa） Chain D 653–794（142 aa）	Not recorded	NWD 3-(5-nitro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-L-alanine × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 3.5；277 K；14-15% PEG 8K, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 3.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.03 Å R-free 0.230
4Q30 Nitrowillardiine bound to the ligand binding domain of GluA2 at pH 3.5 Deposited 2014-04-10	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain F 414–527（114 aa） Chain F 653–794（142 aa）	Not recorded	NWD 3-(5-nitro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-L-alanine × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 3.5；277 K；14-15% PEG 8K, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 3.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.03 Å R-free 0.230
4U1O GluA2flip sLBD complexed with kainate and (R,R)-2b crystal form C Deposited 2014-07-15	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 1 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M Na cacodylate, pH 6.5, 1.26 M ammonium sulfate	Resolution 1.85 Å R-free 0.209
4U1W Full length GluA2-kainate-(R,R)-2b complex crystal form A Deposited 2014-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M MES, pH 6.5, 6%PEG6K, 3% TMAO, 0.006M Taurine	Resolution 3.25 Å R-free 0.316
4U1X Full length GluA2-kainate-(R,R)-2b complex crystal form B Deposited 2014-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M MES, pH 6.2, 5.25% PEG6K, 3% TMAO, 0.006 M Taurine, 20 mM MnCl2	Resolution 3.30 Å R-free 0.289
4U1Y Full length GluA2-FW-(R,R)-2b complex Deposited 2014-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 FWD 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 4 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M imidazole pH 6.2, 9% PEG1450, 3% TMAO	Resolution 3.90 Å R-free 0.303
4U1Z GluA2flip sLBD complexed with kainate and (R,R)-2b crystal form D Deposited 2014-07-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 1 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M Na acetate, pH 4.5, 25% PEG3350	Resolution 1.94 Å R-free 0.208
4U21 GluA2flip sLBD complexed with FW and (R,R)-2b crystal form E Deposited 2014-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 654–796（143 aa） Chain B 413–527（115 aa） Chain B 654–796（143 aa）	Mutation：A796S Mutation：A796S Mutation：A796S Mutation：A796S	FWD 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；phosphate-citrate, pH 4.2, 0.2 M Li sulfate, 20% PEG1K	Resolution 1.39 Å R-free 0.198
4U22 GluA2flip sLBD complexed with FW and (R,R)-2b crystal form D Deposited 2014-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Mutation：A796S Mutation：A796S	FWD 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 1 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M Na acetate, pH 4.5, 20% PEG3K	Resolution 1.44 Å R-free 0.217
4U23 GluA2flip sLBD complexed with FW and (R,R)-2b crystal form F Deposited 2014-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Mutation：A796S Mutation：A796S	FWD 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 1 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M bicine/Trizma base, pH 8.5, 0.09 M Morpheus nitrate-phosphate-sulfate, 10% w/v PEG8K, 20% (v/v) ethylene glycol	Resolution 1.67 Å R-free 0.250
4U2P Full-length AMPA subtype ionotropic glutamate receptor GluA2 in the apo state Deposited 2014-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；0.1 M MES, 5.8-6.2% PEG6000, 5% TMAO, 0.1-0.3 M sodium acetate	Resolution 3.24 Å R-free 0.288
4U2Q Full-length AMPA subtype ionotropic glutamate receptor GluA2 in complex with partial agonist kainate Deposited 2014-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；0.1 M MES, 4.8-5.3% PEG6000, 3.5% TMAO, 6 mM taurine	Resolution 3.52 Å R-free 0.318
4U2R Crystal structure of the GLUR2 ligand binding core (S1S2J, flip variant) in the apo state Deposited 2014-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 413–527（115 aa） Chain A 653–796（144 aa） Chain B 413–527（115 aa） Chain B 653–796（144 aa） Chain C 413–527（115 aa） Chain C 653–796（144 aa） Chain D 413–527（115 aa） Chain D 653–796（144 aa）	Mutation：A796S,A796S Mutation：A796S,A796S Mutation：A796S,A796S Mutation：A796S,A796S Mutation：A796S,A796S Mutation：A796S,A796S Mutation：A796S,A796S Mutation：A796S,A796S	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；297 K；17-20% PEG8000, 0.2M lithium sulfate, 0.1 M sodium acetate	Resolution 1.41 Å R-free 0.232
4U2R Crystal structure of the GLUR2 ligand binding core (S1S2J, flip variant) in the apo state Deposited 2014-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Chain B 653–796（144 aa）	Mutation：A796S,A796S Mutation：A796S,A796S	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；297 K；17-20% PEG8000, 0.2M lithium sulfate, 0.1 M sodium acetate	Resolution 1.41 Å R-free 0.232
4U2R Crystal structure of the GLUR2 ligand binding core (S1S2J, flip variant) in the apo state Deposited 2014-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Mutation：A796S,A796S Mutation：A796S,A796S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；297 K；17-20% PEG8000, 0.2M lithium sulfate, 0.1 M sodium acetate	Resolution 1.41 Å R-free 0.232
4U2R Crystal structure of the GLUR2 ligand binding core (S1S2J, flip variant) in the apo state Deposited 2014-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 413–527（115 aa） Chain C 653–796（144 aa）	Mutation：A796S,A796S Mutation：A796S,A796S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；297 K；17-20% PEG8000, 0.2M lithium sulfate, 0.1 M sodium acetate	Resolution 1.41 Å R-free 0.232
4U2R Crystal structure of the GLUR2 ligand binding core (S1S2J, flip variant) in the apo state Deposited 2014-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 413–527（115 aa） Chain D 653–796（144 aa）	Mutation：A796S,A796S Mutation：A796S,A796S	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；297 K；17-20% PEG8000, 0.2M lithium sulfate, 0.1 M sodium acetate	Resolution 1.41 Å R-free 0.232
4U4F Structure of GluA2* in complex with partial agonist (S)-5-Nitrowillardiine Deposited 2014-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	NWD 3-(5-nitro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-L-alanine × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；11-14% (w/v) PEG 3,000, 50 mM lithium sulfate, 0.1 M tricine	Resolution 4.79 Å R-free 0.262
4U4G Structure of GluA2* in complex with competitive antagonist ZK 200775 Deposited 2014-07-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Fragment：UNP residues 25-847 Chain B 25–847（823 aa） Fragment：UNP residues 25-847 Chain C 25–847（823 aa） Fragment：UNP residues 25-847 Chain D 25–847（823 aa） Fragment：UNP residues 25-847	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	X-RAY DIFFRACTION X-ray crystallization conditions BATCH MODE；277 K；7-11% PEG 20,000, 0.1 M MES	Resolution 4.49 Å R-free 0.248
4U4S Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and BPAM25 at 1.90 A resolution. Deposited 2014-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain A 413–527（115 aa） Fragment：UNP residues 413-527, UNP residues 653-796 Chain A 653–796（144 aa） Fragment：UNP residues 413-527, UNP residues 653-796 Chain B 413–527（115 aa） Fragment：UNP residues 413-527, UNP residues 653-796 Chain B 653–796（144 aa） Fragment：UNP residues 413-527, UNP residues 653-796	Mutation：yes Mutation：yes Mutation：yes Mutation：yes	3C1 4-ethyl-3,4-dihydro-2H-pyrido[4,3-e][1,2,4]thiadiazine 1,1-dioxide × 2 SO4 SULFATE ION × 3 GOL GLYCEROL × 4 ACT ACETATE ION × 8 CL CHLORIDE ION × 2 GLU GLUTAMIC ACID × 2 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；22% PEG4000, 0.2 M ammoniumsulfate, 0.1 M phosphate-citrate.	Resolution 1.90 Å R-free 0.208
4U4X Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and BPAM37 at 1.56 A resolution. Deposited 2014-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain A 413–527（115 aa） Fragment：UNP residues 413-527, UNP residues 653-796 Chain A 653–796（144 aa） Fragment：UNP residues 413-527, UNP residues 653-796 Chain B 413–527（115 aa） Fragment：UNP residues 413-527, UNP residues 653-796 Chain B 653–796（144 aa） Fragment：UNP residues 413-527, UNP residues 653-796	Mutation：yes Mutation：yes Mutation：yes Mutation：yes	3C2 4-ethyl-3,4-dihydro-2H-pyrido[3,2-e][1,2,4]thiadiazine 1,1-dioxide × 2 SO4 SULFATE ION × 5 GLU GLUTAMIC ACID × 2 ACT ACETATE ION × 4 GOL GLYCEROL × 3 PEG DI(HYDROXYETHYL)ETHER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；24% PEG4000, 0.1 M ammoniumsulfate, 0.1 M phosphate-citrate	Resolution 1.56 Å R-free 0.175
4U5B Crystal structure of GluA2 A622T, con-ikot-ikot snail toxin, partial agonist KA and postitive modulator (R,R)-2b complex Deposited 2014-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–845（821 aa） Chain B 25–845（821 aa） Chain C 25–845（821 aa） Chain D 25–845（821 aa）	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M MES pH 5.8-6.3, 0.1 M NaCl, 5%-6% PEG3350	Resolution 3.50 Å R-free 0.261
4U5C Crystal structure of GluA2, con-ikot-ikot snail toxin, partial agonist FW and postitive modulator (R,R)-2b complex Deposited 2014-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–845（821 aa） Chain B 25–845（821 aa） Chain C 25–845（821 aa） Chain D 25–845（821 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 FWD 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 4 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M MES pH 5.8-6.3, 0.1 M NaCl, 5%-6% PEG3350	Resolution 3.69 Å R-free 0.254
4U5D Crystal structure of GluA2, con-ikot-ikot snail toxin, partial agonist KA and postitive modulator (R,R)-2b complex Deposited 2014-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–845（821 aa） Chain B 25–845（821 aa） Chain C 25–845（821 aa） Chain D 25–845（821 aa）	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M MES pH 5.8-6.3, 0.1 M NaCl, 5%-6% PEG3350	Resolution 3.58 Å R-free 0.297
4U5E Crystal structure of GluA2 T625G, con-ikot-ikot snail toxin, partial agonist KA and postitive modulator (R,R)-2b complex Deposited 2014-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–845（821 aa） Chain B 25–845（821 aa） Chain C 25–845（821 aa） Chain D 25–845（821 aa）	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M MES pH 5.8-6.3, 0.1 M NaCl, 5%-6% PEG3350	Resolution 3.51 Å R-free 0.276
4U5F Crystal structure of GluA2, con-ikot-ikot snail toxin, partial agonist KA and postitive modulator (R,R)-2b complex, GluA2cryst2 construct Deposited 2014-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–848（824 aa） Chain B 25–848（824 aa） Chain C 25–848（824 aa） Chain D 25–848（824 aa）	Not recorded	KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1 M MES pH 5.8-6.3, 0.1 M NaCl, 5%-6% PEG3350	Resolution 3.70 Å R-free 0.286
4UQ6 Electron density map of GluA2em in complex with LY451646 and glutamate Deposited 2014-06-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 22–847（826 aa） Fragment：RESIDUES 22-847 Chain B 22–847（826 aa） Fragment：RESIDUES 22-847 Chain C 22–847（826 aa） Fragment：RESIDUES 22-847 Chain D 22–847（826 aa） Fragment：RESIDUES 22-847	Not recorded	GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；ETHANE	Resolution 12.80 Å
4UQJ Cryo-EM density map of GluA2em in complex with ZK200775 Deposited 2014-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 22–847（826 aa） Fragment：RESIDUES 22-847 Chain B 22–847（826 aa） Fragment：RESIDUES 22-847 Chain C 22–847（826 aa） Fragment：RESIDUES 22-847 Chain D 22–847（826 aa） Fragment：RESIDUES 22-847	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	ELECTRON MICROSCOPY cryo-EM buffer 150 MM NACL, 20 MM TRIS, 0.75 MM DDM, 0.12 MM CHS, 0.3 MM ZK200775；pH 8；150 MM NACL, 20 MM TRIS, 0.75 MM DDM, 0.12 MM CHS, 0.3 MM ZK200775 cryo-EM vitrification conditions Cryogen ETHANE；ETHANE	Resolution 10.40 Å
4UQK Electron density map of GluA2em in complex with quisqualate and LY451646 Deposited 2014-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 22–847（826 aa） Fragment：RESIDUES 22-847 Chain B 22–847（826 aa） Fragment：RESIDUES 22-847 Chain C 22–847（826 aa） Fragment：RESIDUES 22-847 Chain D 22–847（826 aa） Fragment：RESIDUES 22-847	Not recorded	QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；ETHANE	Resolution 16.40 Å
4X48 Crystal structure of GluR2 ligand-binding core Deposited 2014-12-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：Ligand binding domain, engineered single chain Chain A 653–796（144 aa） Fragment：Ligand binding domain, engineered single chain Chain C 413–527（115 aa） Fragment：Ligand binding domain, engineered single chain Chain C 653–796（144 aa） Fragment：Ligand binding domain, engineered single chain	Not recorded	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 3 XPF N-{(3S,4S)-4-[4-(5-cyanothiophen-2-yl)phenoxy]tetrahydrofuran-3-yl}propane-2-sulfonamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；The protein solution contained 7 mg/ml GluR2-S1S2J, 10mM (S)-Glu, 10mM HEPES (pH 7.5), 20mM NaCl and 1mM EDTA. Compound was added to a final concentration of 150micromolar from a 30mM DMSO stock. To this solution, an equal amount of reservoir solution containing 10% PEG 8000, 0.1 M ZnAc and 0.1M NaAc, pH 5.5 was added, and 2microlitre drops of this mixture were allowed to equilibrate by vapor diffusion over a 1mL reservoir. Crystals appeared in the drops in 3-5 days.	Resolution 1.89 Å R-free 0.197
4X48 Crystal structure of GluR2 ligand-binding core Deposited 2014-12-02	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：Ligand binding domain, engineered single chain Chain B 653–796（144 aa） Fragment：Ligand binding domain, engineered single chain	Not recorded	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 4 XPF N-{(3S,4S)-4-[4-(5-cyanothiophen-2-yl)phenoxy]tetrahydrofuran-3-yl}propane-2-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；The protein solution contained 7 mg/ml GluR2-S1S2J, 10mM (S)-Glu, 10mM HEPES (pH 7.5), 20mM NaCl and 1mM EDTA. Compound was added to a final concentration of 150micromolar from a 30mM DMSO stock. To this solution, an equal amount of reservoir solution containing 10% PEG 8000, 0.1 M ZnAc and 0.1M NaAc, pH 5.5 was added, and 2microlitre drops of this mixture were allowed to equilibrate by vapor diffusion over a 1mL reservoir. Crystals appeared in the drops in 3-5 days.	Resolution 1.89 Å R-free 0.197
4YMA Structure of the ligand-binding domain of GluA2 in complex with the antagonist CNG10109 Deposited 2015-03-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 6 GOL GLYCEROL × 2 4E5 (3R)-3-(3-carboxy-5-hydroxyphenyl)-L-proline × 2 EDO 1,2-ETHANEDIOL × 2 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；PEG4000, lithium sulfate, phosphate citrate	Resolution 1.90 Å R-free 0.228
4YU0 Crystal structure of a tetramer of GluA2 TR mutant ligand binding domains bound with glutamate at 1.26 Angstrom resolution Deposited 2015-03-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Mutation：E713T, Y768R,E713T, Y768R Mutation：E713T, Y768R,E713T, Y768R	GLU GLUTAMIC ACID × 1 PO4 PHOSPHATE ION × 3 PEG DI(HYDROXYETHYL)ETHER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277.14 K；20% w/v PEG3350 and 200 mM (NH4)2HPO4	Resolution 1.26 Å R-free 0.157
4YU0 Crystal structure of a tetramer of GluA2 TR mutant ligand binding domains bound with glutamate at 1.26 Angstrom resolution Deposited 2015-03-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Chain B 653–796（144 aa）	Mutation：E713T, Y768R,E713T, Y768R Mutation：E713T, Y768R,E713T, Y768R	GLU GLUTAMIC ACID × 1 PO4 PHOSPHATE ION × 3 PEG DI(HYDROXYETHYL)ETHER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277.14 K；20% w/v PEG3350 and 200 mM (NH4)2HPO4	Resolution 1.26 Å R-free 0.157
4Z0I Crystal structure of a tetramer of GluA2 ligand binding domains bound with glutamate at 1.45 Angstrom resolution Deposited 2015-03-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–796（144 aa）	Not recorded	GLU GLUTAMIC ACID × 2 PO4 PHOSPHATE ION × 6 PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277.14 K；20% PEG 3350 and 200 mM KNO3	Resolution 1.45 Å R-free 0.208
4Z0I Crystal structure of a tetramer of GluA2 ligand binding domains bound with glutamate at 1.45 Angstrom resolution Deposited 2015-03-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Chain B 653–796（144 aa）	Not recorded	GLU GLUTAMIC ACID × 2 PO4 PHOSPHATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277.14 K；20% PEG 3350 and 200 mM KNO3	Resolution 1.45 Å R-free 0.208
5BUU Crystal structure of the GluA2 ligand-binding domain (L483Y-N754S) in complex with glutamate and BPAM-321 at 2.07 A resolution Deposited 2015-06-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：UNP residues 413-527,UNP residues 653-796 Chain A 653–796（144 aa） Fragment：UNP residues 413-527,UNP residues 653-796 Chain B 413–527（115 aa） Fragment：UNP residues 413-527,UNP residues 653-796 Chain B 653–796（144 aa） Fragment：UNP residues 413-527,UNP residues 653-796	Mutation：L483Y, N754S,L483Y, N754S Mutation：L483Y, N754S,L483Y, N754S Mutation：L483Y, N754S,L483Y, N754S Mutation：L483Y, N754S,L483Y, N754S	4V6 (3R)-7-chloro-2,3,4-trimethyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide × 2 GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 5 EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；15.2 % PEG4000, 0.2 M ammonium-sulfate, 0.1 M phosphate-citrate	Resolution 2.07 Å R-free 0.250
5CBR Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (S)-2-amino-3-(3,4-dichloro-5-(5-hydroxypyridin-3-yl)phenyl)propanoic acid at 2.0A resolution Deposited 2015-07-01	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Not recorded	4ZK 3,4-dichloro-5-(5-hydroxypyridin-3-yl)-L-phenylalanine × 2 GOL GLYCEROL × 6 SO4 SULFATE ION × 12 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；PEG4000, lithium sulfate and phosphate-citrate buffer pH 4.5	Resolution 2.00 Å R-free 0.238
5CBS Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid at 1.8A resolution Deposited 2015-07-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：UNP residues 413-527,UNP residues 653-797 Chain A 653–797（145 aa） Fragment：UNP residues 413-527,UNP residues 653-797 Chain C 413–527（115 aa） Fragment：UNP residues 413-527,UNP residues 653-797 Chain C 653–797（145 aa） Fragment：UNP residues 413-527,UNP residues 653-797	Not recorded	E42 (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid × 2 SO4 SULFATE ION × 5 EDO 1,2-ETHANEDIOL × 4 GOL GLYCEROL × 3 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；PEG2000, lithium sulfate and phosphate-citrate buffer pH 4.5	Resolution 1.80 Å R-free 0.219
5CBS Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid at 1.8A resolution Deposited 2015-07-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Fragment：UNP residues 413-527,UNP residues 653-797 Chain B 653–797（145 aa） Fragment：UNP residues 413-527,UNP residues 653-797 Chain D 413–527（115 aa） Fragment：UNP residues 413-527,UNP residues 653-797 Chain D 653–797（145 aa） Fragment：UNP residues 413-527,UNP residues 653-797	Not recorded	E42 (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid × 2 SO4 SULFATE ION × 5 EDO 1,2-ETHANEDIOL × 10 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；PEG2000, lithium sulfate and phosphate-citrate buffer pH 4.5	Resolution 1.80 Å R-free 0.219
5ELV Crystal structure of the GluA2 ligand-binding domain (S1S2J-L504-N775) in complex with glutamate and BPAM-521 at 1.92 A resolution Deposited 2015-11-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Fragment：UNP residues, 413-527,UNP residue, 653-797 Chain A 653–797（145 aa） Fragment：UNP residues, 413-527,UNP residue, 653-797 Chain B 413–527（115 aa） Fragment：UNP residues, 413-527,UNP residue, 653-797 Chain B 653–797（145 aa） Fragment：UNP residues, 413-527,UNP residue, 653-797	Mutation：L504Y and N775S Mutation：L504Y and N775S Mutation：L504Y and N775S Mutation：L504Y and N775S	SO4 SULFATE ION × 4 GOL GLYCEROL × 4 CL CHLORIDE ION × 3 ACT ACETATE ION × 9 5PX 4-Cyclopropyl-3,4-dihydro-7-hydroxy-2H-1,2,4-benzothiadiazine 1,1-dioxide × 2 GLU GLUTAMIC ACID × 2 PEG DI(HYDROXYETHYL)ETHER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；20% PEG4000, 0.3 M lithium sulfate and 0.1 M phosphate-citrate	Resolution 1.92 Å R-free 0.209
5FHM Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with (S)-2-Amino-3-(5-(2-(3-(aminomethyl)benzyl)-2H-tetrazol-5-yl)-3-hydroxyisoxazol-4-yl)propanoic acid at resolution 1.55 A resolution Deposited 2015-12-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 6 5XP (2~{S})-3-[5-[2-[[3-(aminomethyl)phenyl]methyl]-1,2,3,4-tetrazol-5-yl]-3-oxidanyl-1,2-oxazol-4-yl]-2-azanyl-propanoic acid × 1 GOL GLYCEROL × 2 ACT ACETATE ION × 4 EDO 1,2-ETHANEDIOL × 7 LI LITHIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；PEG4000 lithium sulfate sodium acetate buffer pH 5.5	Resolution 1.55 Å R-free 0.159
5FHN Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with (S)-2-Amino-3-(5-(2-(3-methylbenzyl)-2H-tetrazol-5-yl)-3-hydroxyisoxazol-4-yl)propanoic acid at 1.6 A resolution Deposited 2015-12-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 1 GOL GLYCEROL × 2 ACT ACETATE ION × 1 5XO (S)-2-Amino-3-(5-(2-(3-methylbenzyl)-2H-tetrazol-5-yl)-3-hydroxyisoxazol-4-yl)propanoic acid × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；18% PEG4000 0.1 M ammonium sulfate 0.1 M phosphate-citrate buffer pH 4.5	Resolution 1.60 Å R-free 0.186
5FHO Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with (S)-2-Amino-3-(5-(2-(3-chlorobenzyl)-2H-tetrazol-5-yl)-3-hydroxyisoxazol-4-yl)propanoic acid at 2.3 A resolution Deposited 2015-12-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain D 413–527（115 aa） Chain D 653–797（145 aa）	Not recorded	5XN (1S)-1-carboxy-2-(5-{2-[(3-chlorophenyl)methyl]-2H-tetrazol-5-yl}-3-oxo-2,3-dihydro-1,2-oxazol-4-yl)ethan-1-aminium × 2 SO4 SULFATE ION × 6 GOL GLYCEROL × 2 CL CHLORIDE ION × 5 EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；PEG4000 ammonium sulfate acetate buffer pH 5.5	Resolution 2.30 Å R-free 0.216
5FHO Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with (S)-2-Amino-3-(5-(2-(3-chlorobenzyl)-2H-tetrazol-5-yl)-3-hydroxyisoxazol-4-yl)propanoic acid at 2.3 A resolution Deposited 2015-12-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Chain B 653–797（145 aa） Chain C 413–527（115 aa） Chain C 653–797（145 aa）	Not recorded	5XN (1S)-1-carboxy-2-(5-{2-[(3-chlorophenyl)methyl]-2H-tetrazol-5-yl}-3-oxo-2,3-dihydro-1,2-oxazol-4-yl)ethan-1-aminium × 2 SO4 SULFATE ION × 6 GOL GLYCEROL × 4 CL CHLORIDE ION × 4 EDO 1,2-ETHANEDIOL × 6 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；280 K；PEG4000 ammonium sulfate acetate buffer pH 5.5	Resolution 2.30 Å R-free 0.216
5FTH Crystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (zinc form) Deposited 2016-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 404–527（124 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796 Chain A 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796 Chain B 404–527（124 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796 Chain B 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；15% PEG 8,000, 200 MM ZN ACETATE, 100MM MES PH 6.0	Resolution 2.90 Å R-free 0.283
5FTH Crystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (zinc form) Deposited 2016-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 404–527（124 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796 Chain C 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796	Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；15% PEG 8,000, 200 MM ZN ACETATE, 100MM MES PH 6.0	Resolution 2.90 Å R-free 0.283
5FTI Crystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (lithium form) Deposited 2016-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 404–527（124 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796 Chain A 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796	Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 LI LITHIUM ION × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；22% PEG 4,000, 200 MM LI SULPHATE, 100MM ACETATE PH 5.0	Resolution 1.35 Å R-free 0.177
5FTI Crystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (lithium form) Deposited 2016-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 404–527（124 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796 Chain B 653–796（144 aa） Fragment：LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796	Mutation：YES Mutation：YES	GLU GLUTAMIC ACID × 2 LI LITHIUM ION × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；22% PEG 4,000, 200 MM LI SULPHATE, 100MM ACETATE PH 5.0	Resolution 1.35 Å R-free 0.177
5FWX Crystal structure of the AMPA receptor GluA2/A4 N-terminal domain heterodimer Deposited 2016-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 25–400（376 aa） Fragment：RESIDUES 25-400	Not recorded	SO4 SULFATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions 17% PEG 3350 WITH 0.1-0.35 M AMMONIUM SULPHATE	Resolution 2.50 Å R-free 0.238
5FWX Crystal structure of the AMPA receptor GluA2/A4 N-terminal domain heterodimer Deposited 2016-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 25–400（376 aa） Fragment：RESIDUES 25-400	Not recorded	SO4 SULFATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions 17% PEG 3350 WITH 0.1-0.35 M AMMONIUM SULPHATE	Resolution 2.50 Å R-free 0.238
5FWY Crystal structure of the AMPA receptor GluA2/A3 N-terminal domain heterodimer Deposited 2016-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 25–400（376 aa） Fragment：RESIDUES 25-400	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 SO4 SULFATE ION × 5 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions 14-16 % PEG 3350, 0.27 M AMMONIUM SULPHATE AND 0.1 M BICINE PH 9	Resolution 2.12 Å R-free 0.231
5FWY Crystal structure of the AMPA receptor GluA2/A3 N-terminal domain heterodimer Deposited 2016-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 25–400（376 aa） Fragment：RESIDUES 25-400	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions 14-16 % PEG 3350, 0.27 M AMMONIUM SULPHATE AND 0.1 M BICINE PH 9	Resolution 2.12 Å R-free 0.231
5IDE Cryo-EM structure of GluA2/3 AMPA receptor heterotetramer (model I) Deposited 2016-02-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 23–883（861 aa） Chain C 23–883（861 aa）	Mutation：N292C Mutation：N292C	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；25 mM Tris pH 7.4, 0.25 % DDM, 150 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；Incubated for 1 minute, blotted for 3 seconds	Resolution 8.25 Å
5IDF Cryo-EM structure of GluA2/3 AMPA receptor heterotetramer (model II) Deposited 2016-02-24	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 23–883（861 aa） Chain C 23–883（861 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；25 mM Tris pH 7.4, 0.25 % DDM, 150 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；Incubated for 1 minute, blotted for 3 seconds	Resolution 10.31 Å
5JEI Crystal structure of the GluA2 LBD in complex with FW Deposited 2016-04-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Mutation：V154C,V154C Mutation：V154C,V154C	FWD 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 4 PO4 PHOSPHATE ION × 8 PG4 TETRAETHYLENE GLYCOL × 8 PEG DI(HYDROXYETHYL)ETHER × 12 TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL × 4 PG0 2-(2-METHOXYETHOXY)ETHANOL × 4 ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 8 EDO 1,2-ETHANEDIOL × 4 NA SODIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；277 K；50.0 % v/v PEG 200, 200 mM Sodium Chloride, 100 mM Sodium/Potassium Phosphate pH 6.2	Resolution 1.23 Å R-free 0.147
5KBS Cryo-EM structure of GluA2-0xSTZ at 8.7 Angstrom resolution Deposited 2016-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Mutation：N241E, V382L, G384E, N385D, V758L,N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L,N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L,N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L,N241E, V382L, G384E, N385D, V758L	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；3 blot force, 8.0 s blot time	Resolution 8.70 Å
5KBT Cryo-EM structure of GluA2-1xSTZ complex at 6.4 Angstrom resolution Deposited 2016-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Mutation：N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；3 blot force, 8.0 s blot time	Resolution 6.40 Å
5KBU Cryo-EM structure of GluA2-2xSTZ complex at 7.8 Angstrom resolution Deposited 2016-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Mutation：N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；3 blot force, 8.0 s blot time	Resolution 7.80 Å
5KBV Cryo-EM structure of GluA2 bound to antagonist ZK200775 at 6.8 Angstrom resolution Deposited 2016-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Mutation：N241E, V382L,G384E, N385D, V758L Mutation：N241E, V382L,G384E, N385D, V758L Mutation：N241E, V382L,G384E, N385D, V758L Mutation：N241E, V382L,G384E, N385D, V758L	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Blot force 3, 8.0 s blot time	Resolution 6.80 Å
5KK2 Architecture of fully occupied GluA2 AMPA receptor - TARP complex elucidated by single particle cryo-electron microscopy Deposited 2016-06-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.30 Å
5L1B AMPA subtype ionotropic glutamate receptor GluA2 in Apo state Deposited 2016-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587,UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain A 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587,UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587,UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587,UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587,UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587,UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587,UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587,UNP residues 25-847, with deletions of 397-398, 402-405, 566-587	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；8-11% (w/v) PEG 8,000, 0.2 M magnesium acetate and 0.1 M sodium cacodylate (pH 6.3-6.7)	Resolution 4.00 Å R-free 0.292
5L1E AMPA subtype ionotropic glutamate receptor GluA2 in complex with noncompetitive inhibitor CP465022 Deposited 2016-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain A 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 6ZQ 3-(2-chlorophenyl)-2-(2-{6-[(diethylamino)methyl]pyridin-2-yl}ethyl)-6-fluoroquinazolin-4(3H)-one × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；11-14% (w/v) PEG 6,000, 0.1 M ammonium phosphate and 0.1 M TRIS (pH 7.9-8.0)	Resolution 4.37 Å R-free 0.292
5L1F AMPA subtype ionotropic glutamate receptor GluA2 in complex with noncompetitive inhibitor Perampanel Deposited 2016-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain A 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 6ZP 2-(6'-oxo-1'-phenyl[1',6'-dihydro[2,3'-bipyridine]]-5'-yl)benzonitrile × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；11-14% (w/v) PEG 6,000, 0.1 M ammonium phosphate and 0.1 M TRIS (pH 7.9-8.0)	Resolution 4.00 Å R-free 0.272
5L1G AMPA subtype ionotropic glutamate receptor GluA2 in complex with GYKI-Br Deposited 2016-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain A 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 GYB (8R)-5-(4-amino-3-bromophenyl)-N,8-dimethyl-8,9-dihydro-2H,7H-[1,3]dioxolo[4,5-h][2,3]benzodiazepine-7-carboxamide × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；sodium acetate	Resolution 4.51 Å R-free 0.295
5L1H AMPA subtype ionotropic glutamate receptor GluA2 in complex with noncompetitive inhibitor GYKI53655 Deposited 2016-07-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain A 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain B 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain C 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 25–565（541 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 Chain D 588–847（260 aa） Fragment：UNP residues 25-847, with deletions of 397-398, 402-405, 566-587	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 GYK (8R)-5-(4-aminophenyl)-N,8-dimethyl-8,9-dihydro-2H,7H-[1,3]dioxolo[4,5-h][2,3]benzodiazepine-7-carboxamide × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；11-14% (w/v) PEG 6,000, 0.1 M ammonium phosphate and 0.1 M TRIS (pH 7.9-8.0)	Resolution 3.80 Å R-free 0.292
5N6P AMPA receptor NTD mutant Deposited 2017-02-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 25–400（376 aa）	Mutation：K73C D134C	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；291 K；16-20% PEG3350, 200 mM sodium formate	Resolution 2.80 Å R-free 0.249
5NG9 Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with agonist CIP-AS at 1.15 A resolution. Deposited 2017-03-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Not recorded	FLC CITRATE ANION × 4 LI LITHIUM ION × 2 8VN (3~{a}~{S},4~{S},6~{a}~{R})-4,5,6,6~{a}-tetrahydro-3~{a}~{H}-pyrrolo[3,4-d][1,2]oxazole-3,4-dicarboxylic acid × 2 8WQ (2~{S},3~{R},4~{R})-3-(carboxycarbonyl)-4-oxidanyl-pyrrolidine-2-carboxylic acid × 2 SO4 SULFATE ION × 6 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；15.2% PEG4000, 0.1 M lithium sulfate, 0.1 M phosphate-citrate buffer	Resolution 1.15 Å R-free 0.133
5NIH Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with agonist LM-12b at 1.3 A resolution. Deposited 2017-03-24	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 3 8VE (3~{a}~{R},4~{S},6~{a}~{R})-1-methyl-4,5,6,6~{a}-tetrahydro-3~{a}~{H}-pyrrolo[3,4-c]pyrazole-3,4-dicarboxylic acid × 1 GOL GLYCEROL × 3 CL CHLORIDE ION × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；24.4% PEG4000, 0.3 M ammonium sulfate, 0.1 M phosphate-citrate buffer	Resolution 1.30 Å R-free 0.158
5NIH Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with agonist LM-12b at 1.3 A resolution. Deposited 2017-03-24	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 2 8VE (3~{a}~{R},4~{S},6~{a}~{R})-1-methyl-4,5,6,6~{a}-tetrahydro-3~{a}~{H}-pyrrolo[3,4-c]pyrazole-3,4-dicarboxylic acid × 1 GOL GLYCEROL × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；24.4% PEG4000, 0.3 M ammonium sulfate, 0.1 M phosphate-citrate buffer	Resolution 1.30 Å R-free 0.158
5NS9 Crystal structure of the GluA2 LBD (L483Y-N754S-L758V) in complex with glutamate Deposited 2017-04-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	1PE PENTAETHYLENE GLYCOL × 2 PG0 2-(2-METHOXYETHOXY)ETHANOL × 1 SO4 SULFATE ION × 6 NA SODIUM ION × 5 GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277.15 K；20% w/v PEG3350, 200mM Li2SO4	Resolution 1.44 Å R-free 0.205
5O9A Crystal structure of the GluA2 ligand-binding domain (S1S2J-L504Y-N775S) in complex with glutamate and BPAM121 at 1.78 A resolution Deposited 2017-06-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Mutation：L504Y,N775S Mutation：L504Y,N775S Mutation：L504Y,N775S Mutation：L504Y,N775S	SO4 SULFATE ION × 6 7M6 7-chloro-4-(2-fluoroethyl)-2,3-dihydro-1,2,4-benzothiadiazine 1,1-dioxide × 2 CL CHLORIDE ION × 4 GOL GLYCEROL × 3 GLU GLUTAMIC ACID × 2 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；18% PEG4000, 0.23 M lithium sulfate, 0.1 M phosphate citrate pH 4.5	Resolution 1.78 Å R-free 0.179
5O9A Crystal structure of the GluA2 ligand-binding domain (S1S2J-L504Y-N775S) in complex with glutamate and BPAM121 at 1.78 A resolution Deposited 2017-06-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Chain C 653–797（145 aa） Chain D 413–527（115 aa） Chain D 653–797（145 aa）	Mutation：L504Y,N775S Mutation：L504Y,N775S Mutation：L504Y,N775S Mutation：L504Y,N775S	SO4 SULFATE ION × 10 7M6 7-chloro-4-(2-fluoroethyl)-2,3-dihydro-1,2,4-benzothiadiazine 1,1-dioxide × 2 CL CHLORIDE ION × 3 GOL GLYCEROL × 1 GLU GLUTAMIC ACID × 2 CIT CITRIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；18% PEG4000, 0.23 M lithium sulfate, 0.1 M phosphate citrate pH 4.5	Resolution 1.78 Å R-free 0.179
5OEW Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with glutamate and positive allosteric modulator BPAM538 Deposited 2017-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 9 ACT ACETATE ION × 2 9TE 4-cyclopropyl-7-(3-methoxyphenoxy)-2,3-dihydro-1$l^{6},2,4-benzothiadiazine 1,1-dioxide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；18% PEG4000, 0.23M lithium-sulfate, 0.1M phosphate-citrate	Resolution 2.00 Å R-free 0.189
5OEW Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with glutamate and positive allosteric modulator BPAM538 Deposited 2017-07-10	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Chain C 653–797（145 aa）	Not recorded	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 16 ACT ACETATE ION × 4 9TE 4-cyclopropyl-7-(3-methoxyphenoxy)-2,3-dihydro-1$l^{6},2,4-benzothiadiazine 1,1-dioxide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；18% PEG4000, 0.23M lithium-sulfate, 0.1M phosphate-citrate	Resolution 2.00 Å R-free 0.189
5VHW GluA2-0xGSG1L bound to ZK Deposited 2017-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.80 Å
5VHX GluA2-1xGSG1L bound to ZK Deposited 2017-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa） Chain E 25–847（823 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.30 Å
5VHY GluA2-2xGSG1L bound to ZK Deposited 2017-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa） Chain E 25–847（823 aa） Chain F 25–847（823 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.60 Å
5VHZ GluA2-2xGSG1L bound to L-Quisqualate Deposited 2017-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa） Chain E 25–847（823 aa） Chain F 25–847（823 aa）	Not recorded	QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.40 Å
5VOT Structure of AMPA receptor-TARP complex Deposited 2017-05-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.90 Å
5VOU Structure of AMPA receptor-TARP complex Deposited 2017-05-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.40 Å
5VOV Structure of AMPA receptor-TARP complex Deposited 2017-05-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.70 Å
5WEK GluA2 bound to antagonist ZK and GSG1L in digitonin, state 1 Deposited 2017-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG Chain B 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG Chain C 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG Chain D 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG	Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.60 Å
5WEL GluA2 bound to antagonist ZK and GSG1L in digitonin, state 2 Deposited 2017-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG Chain B 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG Chain C 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG Chain D 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG	Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 AJP Digitonin × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.40 Å
5WEM GluA2 bound to GSG1L in digitonin, state 1 Deposited 2017-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Fragment：UNP P19491 residues 25-847 and UNP D3Z7H4 residues 2-238 linked via LINKER GTG Chain B 25–847（823 aa） Fragment：UNP P19491 residues 25-847 and UNP D3Z7H4 residues 2-238 linked via LINKER GTG Chain C 25–847（823 aa） Fragment：UNP P19491 residues 25-847 and UNP D3Z7H4 residues 2-238 linked via LINKER GTG Chain D 25–847（823 aa） Fragment：UNP P19491 residues 25-847 and UNP D3Z7H4 residues 2-238 linked via LINKER GTG	Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.10 Å
5WEN GluA2 bound to GSG1L in digitonin, state 2 Deposited 2017-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Fragment：UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG,UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG Chain B 25–847（823 aa） Fragment：UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG,UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG Chain C 25–847（823 aa） Fragment：UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG,UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG Chain D 25–847（823 aa） Fragment：UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG,UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG	Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L,N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L,N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L,N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L,N241E, V382L, G384E, N385D, N392Q, V1151L	AJP Digitonin × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.80 Å
5WEO Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin Deposited 2017-07-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP O88602 2-208 linked via LINKER GT Chain B 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP O88602 2-208 linked via LINKER GT Chain C 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP O88602 2-208 linked via LINKER GT Chain D 25–847（823 aa） Fragment：UNP P19491 residues 25-847, UNP O88602 2-208 linked via LINKER GT	Mutation：N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L Mutation：N241E, V382L, G384E, N385D, V758L	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
6DLZ Open state GluA2 in complex with STZ after micelle signal subtraction Deposited 2018-06-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
6DM0 Open state GluA2 in complex with STZ and blocked by IEM-1460, after micelle signal subtraction Deposited 2018-06-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 GZD N,N,N-trimethyl-5-({[(3s,5s,7s)-tricyclo[3.3.1.1~3,7~]decan-1-yl]methyl}amino)pentan-1-aminium × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.40 Å
6DM1 Open state GluA2 in complex with STZ and blocked by NASPM, after micelle signal subtraction Deposited 2018-06-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 GYY N-[3-({4-[(3-aminopropyl)amino]butyl}amino)propyl]-2-(naphthalen-1-yl)acetamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
6FAZ Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the positive allosteric modulator TDPAM01 at 1.4 A resolution. Deposited 2017-12-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 5 PEG DI(HYDROXYETHYL)ETHER × 2 GOL GLYCEROL × 5 CL CHLORIDE ION × 5 ACT ACETATE ION × 3 GLU GLUTAMIC ACID × 2 EDO 1,2-ETHANEDIOL × 2 D45 6,6'-(Ethane-1,2-diyl)bis(4-methyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide) × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；280 K；15% PEG4000, 0.3 M ammonium sulfate, 0.1 M phosphate-citrate	Resolution 1.40 Å R-free 0.168
6FQG GluA2(flop) G724C ligand binding core dimer bound to L-Glutamate (Form A) at 2.34 Angstrom resolution Deposited 2018-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Mutation：S729C Mutation：S729C Mutation：S729C Mutation：S729C	GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；287 K；0.2M Ammonium chloride, 20% PEG 3350, 10uM ZK200775	Resolution 2.34 Å R-free 0.231
6FQH GluA2(flop) S729C ligand binding core dimer bound to NBQX at 1.76 Angstrom resolution Deposited 2018-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 400–527（128 aa） Chain A 653–797（145 aa） Chain B 400–527（128 aa） Chain B 653–797（145 aa）	Mutation：S729C,S729C Mutation：S729C,S729C Mutation：S729C,S729C Mutation：S729C,S729C	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；289 K；0.1M tri-sodium Citrate, 20% PEG 3000	Resolution 1.76 Å R-free 0.224
6FQI GluA2(flop) G724C ligand binding core dimer bound to L-Glutamate (Form B) at 2.91 Angstrom resolution Deposited 2018-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	GLU GLUTAMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；289 K；0.16 M Calcium acetate, 0.08 M Sodium Cacodylate, 14.4% (w/v) PEG 8000, 20% (v/v) Glycerol, 1 mM glutamate	Resolution 2.91 Å R-free 0.267
6FQJ GluA2(flop) G724C ligand binding core dimer bound to ZK200775 at 2.50 Angstrom resolution Deposited 2018-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain H 413–527（115 aa） Chain H 653–797（145 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；287 K；0.2M Ammonium Chloride, 20% PEG 3350, 10microM ZK200775.	Resolution 2.50 Å R-free 0.265
6FQJ GluA2(flop) G724C ligand binding core dimer bound to ZK200775 at 2.50 Angstrom resolution Deposited 2018-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Chain B 653–797（145 aa） Chain G 413–527（115 aa） Chain G 653–797（145 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；287 K；0.2M Ammonium Chloride, 20% PEG 3350, 10microM ZK200775.	Resolution 2.50 Å R-free 0.265
6FQJ GluA2(flop) G724C ligand binding core dimer bound to ZK200775 at 2.50 Angstrom resolution Deposited 2018-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Chain C 653–797（145 aa） Chain E 413–527（115 aa） Chain E 653–797（145 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；287 K；0.2M Ammonium Chloride, 20% PEG 3350, 10microM ZK200775.	Resolution 2.50 Å R-free 0.265
6FQJ GluA2(flop) G724C ligand binding core dimer bound to ZK200775 at 2.50 Angstrom resolution Deposited 2018-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 413–527（115 aa） Chain D 653–797（145 aa） Chain F 413–527（115 aa） Chain F 653–797（145 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；287 K；0.2M Ammonium Chloride, 20% PEG 3350, 10microM ZK200775.	Resolution 2.50 Å R-free 0.265
6FQK GluA2(flop) S729C ligand binding core dimer bound to ZK200775 at 1.98 Angstrom resolution Deposited 2018-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 400–527（128 aa） Chain A 653–797（145 aa） Chain B 400–527（128 aa） Chain B 653–797（145 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；287 K；0.2M Ammonium Chloride, 20% PEG 3350, 10microM ZK200775.	Resolution 1.98 Å R-free 0.256
6GIV Structure of GluA2-N775S ligand-binding domain (S1S2J) in complex with glutamate and Rubidium Bromide at 1.75 A resolution Deposited 2018-05-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Mutation：N775S,N775S Mutation：N775S,N775S	GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 2 GOL GLYCEROL × 6 BR BROMIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；18-24.4% PEG4000, 0.2-0.3 M Li2SO4, and 0.1 M cacodylate, pH 6.5	Resolution 1.75 Å R-free 0.190
6GL4 Structure of GluA2o ligand-binding domain (S1S2J) in complex with glutamate and sodium bromide at 1.95 A resolution Deposited 2018-05-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 652–797（146 aa）	Not recorded	GLU GLUTAMIC ACID × 2 BR BROMIDE ION × 6 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；25% PEG4000, 0.2M sodium sulfate, 0.1M sodium acetate pH 5.5	Resolution 1.95 Å R-free 0.199
6GL4 Structure of GluA2o ligand-binding domain (S1S2J) in complex with glutamate and sodium bromide at 1.95 A resolution Deposited 2018-05-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Chain B 652–797（146 aa）	Not recorded	GLU GLUTAMIC ACID × 2 BR BROMIDE ION × 6 NA SODIUM ION × 4 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；25% PEG4000, 0.2M sodium sulfate, 0.1M sodium acetate pH 5.5	Resolution 1.95 Å R-free 0.199
6HC9 STRUCTURE OF GLUA2 LIGAND-BINDING DOMAIN (S1S2J-L504Y-N775S) IN COMPLEX WITH GLUTAMATE AND TDPAM02 AT 2.4 A RESOLUTION. Deposited 2018-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	GOL GLYCEROL × 1 CL CHLORIDE ION × 7 GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 8 PEG DI(HYDROXYETHYL)ETHER × 3 PGE TRIETHYLENE GLYCOL × 1 FXW 6,6'-(ETHANE-1,2-DIYL)BIS(4-CYCLOPROPYL-3,4-DIHYDRO-2H-1,2,4-BENZOTHIADIAZINE 1,1-DIOXIDE) × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；20% PEG4000, 0.3 M lithium sulfate, 0.1 M phosphate citrate	Resolution 2.40 Å R-free 0.239
6HCA STRUCTURE OF GLUA2 LIGAND-BINDING DOMAIN (S1S1J) IN COMPLEX WITH POSITIVE ALLOSTERIC MODULATOR TDPAM02 AT 1.8 A RESOLUTION Deposited 2018-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 10 GOL GLYCEROL × 7 CL CHLORIDE ION × 6 FXW 6,6'-(ETHANE-1,2-DIYL)BIS(4-CYCLOPROPYL-3,4-DIHYDRO-2H-1,2,4-BENZOTHIADIAZINE 1,1-DIOXIDE) × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；24% PEG4000, 0.3 M lithium sulfate, 0.1 M phosphate citrate	Resolution 1.88 Å R-free 0.207
6HCB STRUCTURE OF GLUA2 LIGAND-BINDING DOMAIN (S1S2J-N775S) IN COMPLEX WITH GLUTAMATE AND TDPAM01 AT 1.9 A RESOLUTION. Deposited 2018-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 9 GLU GLUTAMIC ACID × 2 GOL GLYCEROL × 4 CL CHLORIDE ION × 4 PEG DI(HYDROXYETHYL)ETHER × 2 D45 6,6'-(Ethane-1,2-diyl)bis(4-methyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide) × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；15% PEG4000, 0.1 M ammonium sulphate, 0.1 M phosphate citrate	Resolution 1.90 Å R-free 0.192
6HCC STRUCTURE OF GLUA2 LIGAND-BINDING DOMAIN (S1S2J-N775S) IN COMPLEX WITH GLUTAMATE AND TDPAM02 AT 1.6 A RESOLUTION. Deposited 2018-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	FXW 6,6'-(ETHANE-1,2-DIYL)BIS(4-CYCLOPROPYL-3,4-DIHYDRO-2H-1,2,4-BENZOTHIADIAZINE 1,1-DIOXIDE) × 1 GLU GLUTAMIC ACID × 2 SO4 SULFATE ION × 5 GOL GLYCEROL × 7 PEG DI(HYDROXYETHYL)ETHER × 2 CL CHLORIDE ION × 3 ACT ACETATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291 K；24% PEG4000, 0.3 M lithium sulfate, 0.1 M phosphate citrate	Resolution 1.62 Å R-free 0.182
6HCH STRUCTURE OF GLUA2 LIGAND-BINDING DOMAIN (S1S2J-L504Y-N775S) IN COMPLEX WITH GLUTAMATE AND TDPAM01 AT 1.6 A RESOLUTION. Deposited 2018-08-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 15 D45 6,6'-(Ethane-1,2-diyl)bis(4-methyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide) × 1 ACT ACETATE ION × 5 GOL GLYCEROL × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；15% PEG4000, 0.1 M zinc acetate, 0.1 M sodium acetate	Resolution 1.60 Å R-free 0.178
6HCH STRUCTURE OF GLUA2 LIGAND-BINDING DOMAIN (S1S2J-L504Y-N775S) IN COMPLEX WITH GLUTAMATE AND TDPAM01 AT 1.6 A RESOLUTION. Deposited 2018-08-15	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Chain C 653–797（145 aa）	Not recorded	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 16 D45 6,6'-(Ethane-1,2-diyl)bis(4-methyl-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide) × 2 ACT ACETATE ION × 6 GOL GLYCEROL × 2 CL CHLORIDE ION × 4 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；15% PEG4000, 0.1 M zinc acetate, 0.1 M sodium acetate	Resolution 1.60 Å R-free 0.178
6NJL Architecture and subunit arrangement of native AMPA receptors Deposited 2019-01-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain B 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.70 Å
6NJM Architecture and subunit arrangement of native AMPA receptors Deposited 2019-01-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain B 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.50 Å
6NJN Architecture and subunit arrangement of native AMPA receptors Deposited 2019-01-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain B 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.50 Å
6O9G Open state GluA2 in complex with STZ and blocked by AgTx-636, after micelle signal subtraction Deposited 2019-03-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 LU7 N~1~-{5-[(3-{[3-(L-arginylamino)propyl]amino}propyl)amino]pentyl}-N~2~-[(2,4-dihydroxyphenyl)acetyl]-L-aspartamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.80 Å
6PEQ GluA2 in complex with its auxiliary subunit CNIH3 - map LBD-TMD-C3 - with antagonist ZK200775 -without NTD Deposited 2019-06-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–868（868 aa） Chain B 1–868（868 aa） Chain C 1–868（868 aa） Chain D 1–868（868 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 PAM PALMITOLEIC ACID × 14 CLR CHOLESTEROL × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.97 Å
6Q54 Structure of GluA2 ligand-binding domain (S1S2J) in complex with the agonist (S)-2-Amino-3-(1-ethyl-4-hydroxy-1H-1,2,3-triazol-5-yl)propanoic acid at 1.4 A resolution Deposited 2018-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 10 HJ8 (2~{S})-2-azanyl-3-(3-ethyl-5-oxidanyl-1,2,3-triazol-4-yl)propanoic acid × 2 GOL GLYCEROL × 4 PGE TRIETHYLENE GLYCOL × 2 CL CHLORIDE ION × 3 CIT CITRIC ACID × 1 LI LITHIUM ION × 3 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；20% PEG4000, 0.3 M lithium sulfate, 0.1 M phosphate-citrate	Resolution 1.40 Å R-free 0.163
6Q60 Structure of GluA2 ligand-binding domain (S1S2J) in complex with the agonist (S)-2-Amino-3-(2-methyl-5-hydroxy-2H-1,2,3-triazol-4-yl)propanoic acid at 1.55 A resolution Deposited 2018-12-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Not recorded	HJH (2~{S})-2-azanyl-3-(2-methyl-5-oxidanyl-1,2,3-triazol-4-yl)propanoic acid × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 12 CL CHLORIDE ION × 3 LI LITHIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；10% PEG4000, 0.1 M lithium sulfate, 0.1 M phosphate-citrate, pH 4.5	Resolution 1.55 Å R-free 0.175
6QKC GluA1/2 In complex with auxiliary subunit gamma-8 Deposited 2019-01-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM TRIS, pH 8, 150 mM NaCl and 0.1 % digitonin (w/v) cryo-EM vitrification conditions Cryogen ETHANE；3uL on grid, 60 sec incubation and 4sec blotting time	Resolution 4.40 Å
6QKZ Full length GluA1/2-gamma8 complex Deposited 2019-01-30	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 22–860（839 aa） Chain D 22–860（839 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM TRIS, pH 8, 150 mM NaCl and 0.1 % digitonin (w/v) cryo-EM vitrification conditions Cryogen ETHANE；3uL on grid, 60 sec incubation and 4sec blotting time	Resolution 6.30 Å
6RUQ Structure of GluA2cryst in complex the antagonist ZK200775 and the negative allosteric modulator GYKI53655 at 4.65 A resolution Deposited 2019-05-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Mutation：N235E, N385D, N392Q, K410A, R586Q, C589A Mutation：N235E, N385D, N392Q, K410A, R586Q, C589A Mutation：N235E, N385D, N392Q, K410A, R586Q, C589A Mutation：N235E, N385D, N392Q, K410A, R586Q, C589A	GYK (8R)-5-(4-aminophenyl)-N,8-dimethyl-8,9-dihydro-2H,7H-[1,3]dioxolo[4,5-h][2,3]benzodiazepine-7-carboxamide × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 6；279 K；0.1 M MES, 12 % PEG 20,000	Resolution 4.65 Å R-free 0.291
6U5S NTD of GluA2 in complex with CNIH3 - with antagonist ZK200775 - in pseudo-symmetric global conformation Deposited 2019-08-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–868（868 aa） Chain B 1–868（868 aa） Chain C 1–868（868 aa） Chain D 1–868（868 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å
6U6I NTD of GluA2 in complex with CNIH3 - with antagonist ZK200775 - in asymmetric global conformation Deposited 2019-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–868（868 aa） Chain B 1–868（868 aa） Chain C 1–868（868 aa） Chain D 1–868（868 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.12 Å
6UCB GluA2 in complex with its auxiliary subunit CNIH3 - with antagonist ZK200775, LBD, TMD, CNIH3, and lipids Deposited 2019-09-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–868（868 aa） Chain B 1–868（868 aa） Chain C 1–868（868 aa） Chain D 1–868（868 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 PAM PALMITOLEIC ACID × 14 CLR CHOLESTEROL × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.28 Å
6UD4 GluA2 in complex with its auxiliary subunit CNIH3 in AS map II - (LBD-TMD-C3(AS) II)- with antagonist ZK200775, without NTD Deposited 2019-09-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–868（868 aa） Chain B 1–868（868 aa） Chain C 1–868（868 aa） Chain D 1–868（868 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 CLR CHOLESTEROL × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
6UD8 GluA2 in complex with its auxiliary subunit CNIH3 - with antagonist ZK200775 Deposited 2019-09-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–868（868 aa） Chain B 1–868（868 aa） Chain C 1–868（868 aa） Chain D 1–868（868 aa）	Not recorded	OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 CLR CHOLESTEROL × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
6XSR Crystal structure of GluA2 AMPA receptor in complex with trans-4-butylcyclohexane carboxylic acid (4-BCCA) inhibitor Deposited 2020-07-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–838（814 aa） Chain B 25–838（814 aa） Chain C 25–838（814 aa） Chain D 25–838（814 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 V8G trans-4-butylcyclohexane-1-carboxylic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；8-11% (w/v) PEG 8,000, 0.2 M magnesium acetate and 0.1 M sodium cacodylate (pH 6.3-6.7) or 11-14% (w/v) PEG 6,000, 0.1 M ammonium phosphate and 0.1 M TRIS (pH 7.9-8.0)	Resolution 4.25 Å R-free 0.296
6YK2 Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the compound (S)-1-[2'-Amino-2'-carboxyethyl]-5,7-dihydrothieno[3,4-d]pyrimidin- 2,4(1H,3H)-dione at resolution 1.60A Deposited 2020-04-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 6 GOL GLYCEROL × 10 CGW (2~{S})-2-azanyl-3-[2,4-bis(oxidanylidene)-5,7-dihydrothieno[3,4-d]pyrimidin-1-yl]propanoic acid × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；15% PEG4000, 0.3M Lithium Sulfate, 0.1M acetate	Resolution 1.61 Å R-free 0.163
6YK3 Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the compound ( S) - 1- [2'-Amino-2'-carboxyethyl]-5 ,7- dihydropyrrolo[3,4-d]pyrimidin-2,4(1H,3H)-dione at resolution 1.20A Deposited 2020-04-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Not recorded	GOL GLYCEROL × 8 SO4 SULFATE ION × 8 PVQ (S)-1-[2'-Amino-2'-carboxyethyl]-5,7-dihydropyrrolo[3,4-d]pyrimidin-2,4(1H,3H)-dione × 2 NH4 AMMONIUM ION × 2 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；20% PEG4000, 0.3M ammonium sulfate, 0.1M acetate	Resolution 1.20 Å R-free 0.140
6YK4 Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the compound ( S) - 1- [2'-Amino-2'-carboxyethyl]-6-methyl-5 ,7- dihydropyrrolo[3,4-d]pyrimidin-2,4(1H,3H)-dione at resolution 1.00A Deposited 2020-04-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 8 GOL GLYCEROL × 8 LI LITHIUM ION × 2 CG8 (2~{S})-2-azanyl-3-[6-methyl-2,4-bis(oxidanylidene)-5,7-dihydropyrrolo[3,4-d]pyrimidin-1-yl]propanoic acid × 2 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；15.2% PEG4000, 0.3M lithium sulfate, 0.1M acetate	Resolution 1.00 Å R-free 0.120
6YK5 Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the compound (S)-1-(2'-Amino-2'-carboxyethyl)-5,7-dihydrofuro[3,4-d]- pyrimidine-2,4(1H,3H)-dione at resolution 1.15A Deposited 2020-04-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Not recorded	GOL GLYCEROL × 8 SO4 SULFATE ION × 12 LI LITHIUM ION × 2 PVK (S)-1-(2'-Amino-2'-carboxyethyl)-5,7-dihydrofuro[3,4-d]-pyrimidine-2,4(1H,3H)-dione × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；279 K；PEG4000, lithium sulfate, acetate	Resolution 1.15 Å R-free 0.130
6YK6 Structure of the AMPA receptor GluA2o ligand-binding domain (S1S2J) in complex with the compound (S)-1-(2'-Amino-2'-carboxyethyl)furo[3,4-d]pyrimidin-2,4-dione at resolution 1.47A Deposited 2020-04-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Not recorded	SO4 SULFATE ION × 8 GOL GLYCEROL × 6 LI LITHIUM ION × 2 CL CHLORIDE ION × 4 OUB (S)-1-(2'-Amino-2'-carboxyethyl)furo[3,4-d]pyrimidin-2,4-dione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；279 K；24.4% PEG4000, 0.15M lithium sulfate, 0.1M phosphate-citrate	Resolution 1.47 Å R-free 0.172
6ZYU Structure of the GluA2 ligand-binding domain (L483Y-N754S) in complex with glutamate and BPAM549 Deposited 2020-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa）	Mutation：L483Y,N754S Mutation：L483Y,N754S	ZN ZINC ION × 4 CAC CACODYLATE ION × 2 ACT ACETATE ION × 4 GLU GLUTAMIC ACID × 2 QSZ (4~{S})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide × 2 QSW (4~{R})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide × 2 GOL GLYCEROL × 6 CL CHLORIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；299 K；Zinc acetate, polyethylene glycol 4000, cacodylate	Resolution 1.90 Å R-free 0.187
6ZYU Structure of the GluA2 ligand-binding domain (L483Y-N754S) in complex with glutamate and BPAM549 Deposited 2020-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 413–527（115 aa） Chain B 653–797（145 aa） Chain C 413–527（115 aa） Chain C 653–797（145 aa）	Mutation：L483Y,N754S Mutation：L483Y,N754S Mutation：L483Y,N754S Mutation：L483Y,N754S	ZN ZINC ION × 6 ACT ACETATE ION × 3 GLU GLUTAMIC ACID × 2 QSZ (4~{S})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide × 2 QSW (4~{R})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide × 2 GOL GLYCEROL × 3 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；299 K；Zinc acetate, polyethylene glycol 4000, cacodylate	Resolution 1.90 Å R-free 0.187
7OCA Resting state full-length GluA1/A2 heterotertramer in complex with TARP gamma 8 and CNIH2 Deposited 2021-04-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 46 CLR CHOLESTEROL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7OCC NTD of resting state GluA1/A2 heterotertramer Deposited 2021-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–860（860 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7OCC NTD of resting state GluA1/A2 heterotertramer Deposited 2021-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–860（860 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7OCD Resting state GluA1/A2 heterotetramer in complex with auxiliary subunit TARP gamma 8 (LBD-TMD) Deposited 2021-04-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
7OCE Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and CNIH2 (LBD-TMD) Deposited 2021-04-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 46 CLR CHOLESTEROL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
7OCF Active state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and CNIH2 (LBD-TMD) Deposited 2021-04-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	CYZ CYCLOTHIAZIDE × 4 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 26 GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7QHB Active state of GluA1/2 in complex with TARP gamma 8, L-glutamate and CTZ Deposited 2021-12-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	PAM PALMITOLEIC ACID × 14 GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 79N (2S)-2,3-dihydroxypropyl (7Z)-hexadec-7-enoate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM TRIS 150 mM NaCl 0.02 % GDN 87 uM CTZ 100 mM L-Glu cryo-EM vitrification conditions Cryogen ETHANE；3-4 second blots	Resolution 3.50 Å
7QHH Desensitized state of GluA1/2 AMPA receptor in complex with TARP-gamma 8 (TMD-LBD) Deposited 2021-12-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	GLU GLUTAMIC ACID × 4 PAM PALMITOLEIC ACID × 10 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 79N (2S)-2,3-dihydroxypropyl (7Z)-hexadec-7-enoate × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM TRIS 150 mM NaCl 0.02 % GDN 87 uM CTZ 100 mM L-Glu cryo-EM vitrification conditions Cryogen ETHANE；3-4 second blots	Resolution 3.60 Å
7RYY Structure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist glutamate Deposited 2021-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；25 mM glutamate was added to the purified protein and incubated on ice for 30 min before sample preparation	Resolution 4.40 Å
7RYZ Structure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit GSG1L bound to agonist quisqualate Deposited 2021-08-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；1mM Quisqualate was added to the purified protein and incubated on ice for 30 min before sample preparation	Resolution 4.15 Å
7RZ4 Structure of the complex of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK 200775 Deposited 2021-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 24	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；0.1mM ZK was added to the purified protein and incubated on ice for 30 min before sample preparation	Resolution 3.60 Å
7RZ5 Structure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK 200775 Deposited 2021-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 24	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；0.1mM ZK was added to the purified protein and incubated on ice for 30 min before sample preparation	Resolution 3.30 Å
7RZ6 Structure of the complex of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist glutamate Deposited 2021-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；25 mM glutamate was added to the purified protein and incubated on ice for 30 min before sample preparation	Resolution 4.40 Å
7RZ7 Structure of the complex of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist Quisqualate Deposited 2021-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；1 mM Quisqualate was added to the purified protein and incubated on ice for 30 min before sample preparation	Resolution 4.20 Å
7RZ8 Structure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist quisqualate Deposited 2021-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 22 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；1 mM Quisqualate was added to the purified protein and incubated on ice for 30 min before sample preparation	Resolution 4.10 Å
7RZ9 Structure of the complex of AMPA receptor GluA2 with auxiliary subunit GSG1L in the apo state Deposited 2021-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.15 Å
7RZA Structure of the complex of AMPA receptor GluA2 with auxiliary subunit GSG1L bound to agonist quisqualate Deposited 2021-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；1mM Quisqualate was added to the purified protein and incubated on ice for 30 min before sample preparation	Resolution 4.26 Å
7TNK Complex GNNN of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2 (Stargazin) at low glutamate concentration (20 uM) in the presence of cyclothiazide (100 uM) Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 1 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å
7TNL Complex GNGN1 of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2 (Stargazin) at low glutamate concentration (20 uM) in the presence of cyclothiazide (100 uM) Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 2 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.59 Å
7TNM Complex GNGN2 of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2 (Stargazin) at low glutamate concentration (20 uM) in the presence of cyclothiazide (100 uM) Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 2 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.74 Å
7TNN Complex GGNN of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2 (Stargazin) at low glutamate concentration (20 uM) in the presence of cyclothiazide (100 uM) Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 2 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.91 Å
7TNO Complex GGGN of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2 (Stargazin) at low glutamate concentration (20 uM) in the presence of cyclothiazide (100 uM) Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 3 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.02 Å
7TNP Complex GGGG of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2 (Stargazin) at low glutamate concentration (20 uM) in the presence of cyclothiazide (100 uM) Deposited 2022-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.96 Å
8AYL Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand JNJ-61432059 Deposited 2022-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 PLM PALMITIC ACID × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 OIJ 5-[2-(4-fluorophenyl)-7-(4-oxidanylpiperidin-1-yl)pyrazolo[1,5-c]pyrimidin-3-yl]-1,3-dihydroindol-2-one × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8AYM Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand JNJ-55511118 Deposited 2022-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	XVD 6-[2-chloro-6-(trifluoromethoxy)phenyl]-1H-benzimidazol-2-ol × 2 PLM PALMITIC ACID × 14 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8AYN Resting state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand LY3130481 Deposited 2022-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 PLM PALMITIC ACID × 14 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4 OLR 6-[(1~{S})-1-[1-[5-(2-hydroxyethyloxy)pyridin-2-yl]pyrazol-3-yl]ethyl]-3~{H}-1,3-benzothiazol-2-one × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
8AYO Open state GluA1/A2 AMPA receptor in complex with TARP gamma 8 and ligand JNJ-61432059 Deposited 2022-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–860（860 aa） Chain D 1–860（860 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 PLM PALMITIC ACID × 10 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 2 OIJ 5-[2-(4-fluorophenyl)-7-(4-oxidanylpiperidin-1-yl)pyrazolo[1,5-c]pyrimidin-3-yl]-1,3-dihydroindol-2-one × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
8C1R Resting state homomeric GluA2 F231A mutant AMPA receptor in complex with TARP gamma-2 Deposited 2022-12-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PLM PALMITIC ACID × 7 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8C1S Transmembrane domain of resting state homomeric GluA2 F231A mutant AMPA receptor in complex with TARP gamma 2 Deposited 2022-12-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8FP4 GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 500mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na610) Deposited 2023-01-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain B 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain C 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain D 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification	Not recorded	CL CHLORIDE ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.40 Å
8FP9 GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100mM glutamate (Open-CaNaMg) Deposited 2023-01-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion	CA CALCIUM ION × 1 CL CHLORIDE ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100 mM) and cyclothiazide (CTZ, 0.33 mM) were added before freezing. The 1 M L-glutamic acid stock solution was adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.44 Å
8FPC Conformation 1 of the ligand binding domain (LBDconf1) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100mM glutamate (Open-CaNaMg) Deposited 2023-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100 mM) and cyclothiazide (CTZ, 0.33 mM) were added before freezing. The 1 M L-glutamic acid stock solution was adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.78 Å
8FPG GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100uM CNQX (Closed-CaNaMg) Deposited 2023-01-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion	CL CHLORIDE ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；6-cyano-7-nitroquinoxaline-2,3-dione (CNQX, 0.1 mM) and cyclothiazide (CTZ, 0.33 mM) were added before freezing. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.32 Å
8FPH Conformation 2 of the ligand binding domain (LBDconf2) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100mM glutamate (Open-CaNaMg) Deposited 2023-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100 mM) and cyclothiazide (CTZ, 330 uM) were added before freezing. The 1 M L-glutamic acid stock solution was adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
8FPK LBD conformation 1 of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100uM CNQX (Closed-CaNaMg) Deposited 2023-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion	Y4Y 6-(aminomethyl)-7-nitro-1,4-dihydroquinoxaline-2,3-dione × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；6-cyano-7-nitroquinoxaline-2,3-dione (CNQX, 0.1 mM) and cyclothiazide (CTZ, 0.33 mM) were added before freezing. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.76 Å
8FPL LBD conformation 2 (LBDconf2) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100uM CNQX (Closed-CaNaMg) Deposited 2023-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion Mutation：FLAG epitope tag (DYKDDDDK) insertion	Y4Y 6-(aminomethyl)-7-nitro-1,4-dihydroquinoxaline-2,3-dione × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；6-cyano-7-nitroquinoxaline-2,3-dione (CNQX, final conc. 0.1mM) and cyclothiazide (CTZ, final conc. 0.33mM) was added before freezing. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.81 Å
8FPS GluA2 flip Q isoform N619K mutant of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100mM glutamate (Open-CaNaMg/N619K) Deposited 2023-01-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain B 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain C 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain D 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification	Mutation：N619K Mutation：N619K Mutation：N619K Mutation：N619K	CL CHLORIDE ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.38 Å
8FPV LBD conformation 1 (LBDconf1) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 500mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na610) Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.08 Å
8FPY LBD conformation 2 (LBDconf2) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 500mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na610) Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.98 Å
8FPZ LBD conformation 3 (LBDconf3) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 500mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na610) Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.01 Å
8FQ1 GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with 150mM CaCl2, 330uM CTZ, and 100mM L-glutamate (Open-Ca150) Deposited 2023-01-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain B 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain C 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain D 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.59 Å
8FQ2 LBD conformation 1 (LBDconf1) of GluA2 flip Q isoform N619K mutant of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100mM glutamate (Open-CaNaMg/N619K) Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain B 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain C 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain D 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification	Mutation：N619K Mutation：N619K Mutation：N619K Mutation：N619K	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
8FQ3 LBD conformation 2 (LBDconf2) of GluA2 flip Q isoform N619K mutant of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100mM glutamate (Open-CaNaMg/N619K) Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain B 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain C 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain D 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification	Mutation：N619K Mutation：N619K Mutation：N619K Mutation：N619K	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.17 Å
8FQ5 GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with 140mM NMDG, 330uM CTZ, and 100mM L-glutamate (Open-Na110) Deposited 2023-01-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	CL CHLORIDE ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.34 Å
8FQ6 LBD of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with 150mM CaCl2, 330uM CTZ, and 100mM L-glutamate (Open-Ca150) Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain B 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain C 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain D 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
8FQ8 LBD conformation 1 (LBDconf1) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with 140mM NMDG, 330uM CTZ, and 100mM L-glutamate (Open-Na110) Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) were added before freezing. The 1 M L-glutamic acid stock solution was adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.11 Å
8FQA LBD conformation 2 (LBDconf2) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with 140mM NMDG, 330uM CTZ, and 100mM L-glutamate (Open-Na110) Deposited 2023-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.35 Å
8FQB GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with 10mM CaCl2, 140mM NMDG, 330uM CTZ, and 100mM L-glutamate (Open-Ca10) Deposited 2023-01-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain B 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain C 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Chain D 1–883（883 aa） Fragment：DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.36 Å
8FQD LBD conformation 1 (LBDconf1) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with 10mM CaCl2, 140mM NMDG, 330uM CTZ, and 100mM L-glutamate (Open-Ca10) Deposited 2023-01-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.01 Å
8FQE LBD conformation 2 (LBDconf2) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma2, with 10mM CaCl2, 140mM NMDG, 330uM CTZ, and 100mM L-glutamate (Open-Ca10) Deposited 2023-01-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
8FQF GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 150mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na260) Deposited 2023-01-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	CL CHLORIDE ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.29 Å
8FQG LBD conformation 1 (LBDconf1) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 150mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na260) Deposited 2023-01-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.01 Å
8FQH LBD conformation 2 (LBDconf2) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 150mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na260) Deposited 2023-01-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.43 Å
8FR0 LBD conformation 3 (LBDconf3) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 150mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na260) Deposited 2023-01-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.04 Å
8P3Q Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 3 Deposited 2023-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	PLM PALMITIC ACID × 7 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.95 Å
8P3S Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 2 Deposited 2023-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	PLM PALMITIC ACID × 7 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.95 Å
8P3X Homomeric GluA2 flip R/G-edited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 1 Deposited 2023-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Mutation：F231A Mutation：F231A Mutation：F231A Mutation：F231A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.36 Å
8P3Y Homomeric GluA2 flip R/G-edited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 3 Deposited 2023-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Mutation：F231A Mutation：F231A Mutation：F231A Mutation：F231A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.55 Å
8P3Z Homomeric GluA2 flip R/G-edited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 2 Deposited 2023-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Mutation：F231A Mutation：F231A Mutation：F231A Mutation：F231A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.46 Å
8QEZ Crystal structure of the AMPA receptor GluA2-L504Y-N775S ligand binding domain in complex with L-glutamate and positive allosteric modulator BPAM395 at 1.55A resolution Deposited 2023-09-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 413–527（115 aa） Chain A 653–797（145 aa） Chain B 413–527（115 aa） Chain B 653–797（145 aa）	Mutation：L504Y,N775S Mutation：L504Y,N775S Mutation：L504Y,N775S Mutation：L504Y,N775S	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 5 ACT ACETATE ION × 7 UF5 6-chloranyl-4-cyclopropyl-2,3-dihydrothieno[3,2-e][1,2,4]thiadiazine 1,1-dioxide × 2 CL CHLORIDE ION × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；15.2% PEG4000, 0.1M Zn Acetate, 0.1M Cacodylate pH 6.5	Resolution 1.55 Å R-free 0.195
8QEZ Crystal structure of the AMPA receptor GluA2-L504Y-N775S ligand binding domain in complex with L-glutamate and positive allosteric modulator BPAM395 at 1.55A resolution Deposited 2023-09-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 413–527（115 aa） Chain C 653–797（145 aa）	Mutation：L504Y,N775S Mutation：L504Y,N775S	GLU GLUTAMIC ACID × 2 ZN ZINC ION × 4 ACT ACETATE ION × 2 UF5 6-chloranyl-4-cyclopropyl-2,3-dihydrothieno[3,2-e][1,2,4]thiadiazine 1,1-dioxide × 2 CL CHLORIDE ION × 2 GOL GLYCEROL × 6 CAC CACODYLATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；279 K；15.2% PEG4000, 0.1M Zn Acetate, 0.1M Cacodylate pH 6.5	Resolution 1.55 Å R-free 0.195
8SS2 Structure of AMPA receptor GluA2 complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to competitive antagonist ZK and channel blocker spermidine (closed state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 26 CLR CHOLESTEROL × 2 AJP Digitonin × 2 SPD SPERMIDINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 3.58 Å
8SS3 Structure of LBD-TMD of AMPA receptor GluA2 in complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to competitive antagonist ZK and channel blocker spermidine (closed state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 50 CLR CHOLESTEROL × 4 AJP Digitonin × 6 SPD SPERMIDINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 3.21 Å
8SS4 Structure of LBD-TMD of AMPA receptor GluA2 in complex with auxiliary subunits TARP gamma-5 and cornichon-2 (apo state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	SPD SPERMIDINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 3.30 Å
8SS5 Structure of LBD-TMD of AMPA receptor GluA2 in complex with auxiliary subunit TARP gamma-5 (apo state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 3.56 Å
8SS6 Structure of AMPA receptor GluA2 complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to competitive antagonist ZK, channel blocker spermidine and antiepileptic drug perampanel (closed state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	6ZP 2-(6'-oxo-1'-phenyl[1',6'-dihydro[2,3'-bipyridine]]-5'-yl)benzonitrile × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 28 CLR CHOLESTEROL × 8 NA SODIUM ION × 1 SPD SPERMIDINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 3.01 Å
8SS7 Structure of AMPA receptor GluA2 complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to competitive antagonist ZK, channel blocker spermidine and antiepileptic drug perampanel (closed state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	6ZP 2-(6'-oxo-1'-phenyl[1',6'-dihydro[2,3'-bipyridine]]-5'-yl)benzonitrile × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 28 CLR CHOLESTEROL × 8 NA SODIUM ION × 1 SPD SPERMIDINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 2.76 Å
8SS8 Structure of AMPA receptor GluA2 complex with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK and antiepileptic drug perampanel (closed state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	6ZP 2-(6'-oxo-1'-phenyl[1',6'-dihydro[2,3'-bipyridine]]-5'-yl)benzonitrile × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 14 NA SODIUM ION × 2 CLR CHOLESTEROL × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 2.81 Å
8SS9 Structure of LBD-TMD of AMPA receptor GluA2 in complex with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK and antiepileptic drug perampanel (closed state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	6ZP 2-(6'-oxo-1'-phenyl[1',6'-dihydro[2,3'-bipyridine]]-5'-yl)benzonitrile × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 14 CLR CHOLESTEROL × 2 NA SODIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 2.72 Å
8SSA Structure of AMPA receptor GluA2 complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to glutamate and channel blocker spermidine (desensitized state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 12 GLU GLUTAMIC ACID × 4 SPD SPERMIDINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 3.88 Å
8SSB Structure of LBD-TMD of AMPA receptor GluA2 in complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to glutamate and channel blocker spermidine (desensitized state) Deposited 2023-05-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 28 GLU GLUTAMIC ACID × 4 SPD SPERMIDINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；vitrification carried out in nitrogen atmosphere	Resolution 3.66 Å
8VJ6 GluA2 bound to GYKI-52466 and Glutamate, Inhibited State 1 Deposited 2024-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–842（818 aa） Chain B 25–842（818 aa） Chain C 25–842（818 aa） Chain D 25–842（818 aa）	Not recorded	A1AB5 4-[(5S,8R)-8-methyl-6,7,8,9-tetrahydro-2H,5H-[1,3]dioxolo[4,5-h][2,3]benzodiazepin-5-yl]aniline × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8VJ7 GluA2 bound to GYKI-52466 and Glutamate, Inhibited State 2 Deposited 2024-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–842（818 aa） Chain B 25–842（818 aa） Chain C 25–842（818 aa） Chain D 25–842（818 aa）	Not recorded	GLU GLUTAMIC ACID × 4 A1AB5 4-[(5S,8R)-8-methyl-6,7,8,9-tetrahydro-2H,5H-[1,3]dioxolo[4,5-h][2,3]benzodiazepin-5-yl]aniline × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.85 Å
9B5Z GluA2 flip Q in complex with TARPgamma2 at pH8, consensus structure of LBD-TMD-TARPgamma2 Deposited 2024-03-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris adjusted to pH 8 using HCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.71 Å
9B60 GluA2 flip Q in complex with TARPgamma2 at pH8, consensus structure of TMD-TARPgamma2 Deposited 2024-03-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris adjusted to pH 8 using HCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.57 Å
9B61 GluA2 flip Q in complex with TARPgamma2 at pH5, consensus structure of LBD-TMD-TARPgamma2 Deposited 2024-03-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris adjusted to pH 8 using HCl. 4 micro litter of protein in buffer was mixed with 1 micro litter of 50mM citric acid buffer (the 50mM citric acid buffer was prepared by diluting 0.5M citric acid/sodium citrate buffer at pH4.0) immediately before applying the sample to the grid. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.81 Å
9B63 GluA2 flip Q in complex with TARPgamma2 at pH5, consensus structure of TMD-TARPgamma2 Deposited 2024-03-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris adjusted to pH 8 using HCl. 4 micro litter of protein in buffer was mixed with 1 micro litter of 50mM citric acid buffer (the 50mM citric acid buffer was prepared by diluting 0.5M citric acid/sodium citrate buffer at pH4.0) immediately before applying the sample to the grid. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.76 Å
9B64 GluA2 flip Q in complex with TARPgamma2 at pH5, class23, structure of LBD-TMD-TARPgamma2 Deposited 2024-03-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris adjusted to pH 8 using HCl. 4 micro litter of protein in buffer was mixed with 1 micro litter of 50mM citric acid buffer (the 50mM citric acid buffer was prepared by diluting 0.5M citric acid/sodium citrate buffer at pH4.0) immediately before applying the sample to the grid. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.56 Å
9B67 GluA2 flip Q in complex with TARPgamma2 at pH8, class1, structure of LBD-TMD-TARPgamma2 Deposited 2024-03-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris adjusted to pH 8 using HCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.39 Å
9B68 GluA2 flip Q in complex with TARPgamma2 at pH8, class1, structure of NTD Deposited 2024-03-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris adjusted to pH 8 using HCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9B69 GluA2 flip Q in complex with TARPgamma2 at pH8, class12, structure of NTD Deposited 2024-03-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris adjusted to pH 8 using HCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.69 Å
9B6A GluA2 flip Q in complex with TARPgamma2 at pH8, class12, structure of LBD-TMD-TARPgamma2 Deposited 2024-03-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–883（883 aa） Chain B 1–883（883 aa） Chain C 1–883（883 aa） Chain D 1–883（883 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8；Tris adjusted to pH 8 using HCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.35 Å
9DHP Resting state 1 of the GluA2-gamma2 complex Deposited 2024-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 412–841（430 aa） Chain B 412–841（430 aa） Chain C 412–841（430 aa） Chain D 412–841（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.18 Å
9DHQ Resting state 2 of the GluA2-gamma2 complex Deposited 2024-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 412–841（430 aa） Chain B 412–841（430 aa） Chain C 412–841（430 aa） Chain D 412–841（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.78 Å
9DHR Glutamate activated state of the GluA2-gamma2 complex Deposited 2024-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 412–841（430 aa） Chain B 412–841（430 aa） Chain C 412–841（430 aa） Chain D 412–841（430 aa）	Not recorded	GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.54 Å
9DHS Desensitized state 1 of the GluA2-gamma2 complex Deposited 2024-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 412–841（430 aa） Chain B 412–841（430 aa） Chain C 412–841（430 aa） Chain D 412–841（430 aa）	Not recorded	GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.48 Å
9DHT Desensitized state 2 of the GluA2-gamma2 complex Deposited 2024-09-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 412–841（430 aa） Chain B 412–841（430 aa） Chain C 412–841（430 aa） Chain D 412–841（430 aa）	Not recorded	GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.31 Å
9E4Y GluA2-gamma2 complex bound to memantine, glutamate, and cyclothiazide Deposited 2024-10-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 25–841（817 aa） Chain B 25–841（817 aa） Chain C 25–841（817 aa） Chain D 25–841（817 aa）	Not recorded	377 Memantine × 1 GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
9E4Z GluA2-gamma2 complex bound glutamate and cyclothiazide Deposited 2024-10-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 25–841（817 aa） Chain B 25–841（817 aa） Chain C 25–841（817 aa） Chain D 25–841（817 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
9E9D Structure of full length AMPA receptor GluA2 and auxiliary subunit TARP gamma-2 in complex with anti-miR 17 oligonucleotide RGLS4326 Deposited 2024-11-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Not recorded	A1BX3 O-{[(1S,3S,4R,6S,7R)-7-{[(R)-{[(1R,3R,4R,6S,7R)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-7-hydroxy-6-methyl-2,5-dioxabicyclo[2.2.1]heptan-1-yl]methoxy}(sulfanyl)phosphoryl]oxy}-3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-6-methyl-2,5-dioxabicyclo[2.2.1]heptan-1-yl]methyl} O-[(2R,3S,4R,5S)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-methoxy-2-methyloxolan-3-yl] hydrogen (R)-phosphorothioate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å
9E9E Structure of AMPA receptor GluA2 and auxiliary subunit TARP gamma-2 (LBD-TMD) in complex with anti-miR 17 oligonucleotide RGLS4326 Deposited 2024-11-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 25–847（823 aa） Chain B 25–847（823 aa） Chain C 25–847（823 aa） Chain D 25–847（823 aa）	Mutation：N48D Mutation：N48D Mutation：N48D Mutation：N48D	A1BX3 O-{[(1S,3S,4R,6S,7R)-7-{[(R)-{[(1R,3R,4R,6S,7R)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-7-hydroxy-6-methyl-2,5-dioxabicyclo[2.2.1]heptan-1-yl]methoxy}(sulfanyl)phosphoryl]oxy}-3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-6-methyl-2,5-dioxabicyclo[2.2.1]heptan-1-yl]methyl} O-[(2R,3S,4R,5S)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-methoxy-2-methyloxolan-3-yl] hydrogen (R)-phosphorothioate × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å
9MRK Glutamate activated state of the GluA2-gamma2 complex prepared at 37 degrees C Deposited 2025-01-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 412–841（430 aa） Chain B 412–841（430 aa） Chain C 412–841（430 aa） Chain D 412–841（430 aa）	Not recorded	GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.62 Å
9MRL Desensitized state 1 of the GluA2-gamma2 complex prepared at 37 degrees C Deposited 2025-01-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 412–841（430 aa） Chain B 412–841（430 aa） Chain C 412–841（430 aa） Chain D 412–841（430 aa）	Not recorded	GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.17 Å
9MRM Desensitized state 2 of the GluA2-gamma2 complex prepared at 37 degrees C Deposited 2025-01-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 412–841（430 aa） Chain B 412–841（430 aa） Chain C 412–841（430 aa） Chain D 412–841（430 aa）	Not recorded	GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.52 Å
9MRN Consensus glutamate activated state of the GluA2-gamma2 complex Deposited 2025-01-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 412–841（430 aa） Chain B 412–841（430 aa） Chain C 412–841（430 aa） Chain D 412–841（430 aa）	Not recorded	GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.46 Å
9OVT Heteromeric GluA1/A2 in the inactive state, composite map of LBD-TMD Deposited 2025-05-31	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 413–841（429 aa） Chain D 413–841（429 aa）	Not recorded	ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NA SODIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8；150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 100 uM ZK-200775 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.43 Å
9OVU Composite map of GluA1/A2 in the activated state, in complex with positive allosteric modulator (R,R)-2b and agonist glutamate (ATD-LBD-TMD) Deposited 2025-05-31	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–847（847 aa） Chain D 1–847（847 aa）	Not recorded	GLU GLUTAMIC ACID × 4 NA SODIUM ION × 1 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8；150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 500 uM (R,R)-2b, 1 mM glutamate cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9OVW Heteromeric GluA1/A2 in the desensitized state, composite map of ATD-LBD-TMD Deposited 2025-05-31	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 25–841（817 aa） Chain D 25–841（817 aa）	Not recorded	QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 1 mM quiqualate cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.91 Å

333 other PDB entries and 482 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GRIA2_RAT
Isoform	P19491-2
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–428； UniProt 413–840 Author chain D； PDBConstruct 1–428； UniProt 413–840

Protein cornichon homolog 1

OrganismNot specified

UniProt O95406

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain E； UniProt 2–143 Chain F； UniProt 2–143 Chain G； UniProt 2–143 Chain H； UniProt 2–143	Not recorded	Isoform Flip of Glutamate receptor 1 × 2 （P19490） Isoform Flip of Glutamate receptor 2 × 2 （P19491） GLU GLUTAMIC ACID × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 16 FWF N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide × 2 NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8；150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 500 uM (R,R)-2b, 1 mM glutamate cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.76 Å

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	CNIH1_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain E； PDBConstruct 1–142； UniProt 2–143 Author chain F； PDBConstruct 1–142； UniProt 2–143 Author chain G； PDBConstruct 1–142； UniProt 2–143 Author chain H； PDBConstruct 1–142； UniProt 2–143

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9ovv
Deposition date deposition_date	2025-05-31
Structure title title	Heteromeric GluA1/A2-CNIH1 in the activated state, composite map of LBD-TMD
Keywords keywords	GluA1A2-CNIH2 heterotetramer active iGluR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	48.03 Å
Radius of gyration Rg (electron density) rg_electron	46.89 Å
Forward intensity I(0) i0	788446000.00
Molecular weight molecular_weight	259600.0 kDa
Excluded volume excluded_volume	335710 Å³
Envelope volume envelope_volume	472420 Å³
Hydration-shell volume shell_volume	82920 Å³
Envelope diameter envelope_diameter	156.6 Å
Shell Rg shell_rg	52.41 Å
Envelope Rg envelope_rg	45.80 Å
Shape Rg shape_rg	46.91 Å
Total Rg total_rg	47.06 Å
Total atoms total_atoms	35769
Residues n_residues	2182
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	154.9 Å
Rg (real space) rg_real	47.81 Å
Rg uncertainty (real space) rg_real_error	1.16 Å
I(0) (real space) i0_real	7.8840e+08
I(0) uncertainty (real space) i0_real_error	1.2520e+07
Rg (reciprocal space) rg_reciprocal	48.03 Å
I(0) (reciprocal space) i0_reciprocal	788700000.0000
Solution quality estimate total_estimate	0.9012
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	61.0 Å
Skewness Skewness skewness	0.138
Kurtosis Kurtosis kurtosis	-0.587
Angular range angular_range	— – 0.1650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	61520000.0000
Real-space data points n_real_points	34
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.929

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Isoform Flip of Glutamate receptor 1
Molecular weight formula_weight	48285.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	35769

SVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRGPVNLAVLKLSEQGVLDKLKSKWWYDKGECGSKDSGSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSR

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Isoform Flip of Glutamate receptor 2
Molecular weight formula_weight	47767.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

QKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMRQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSR

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	Protein cornichon homolog 1
Molecular weight formula_weight	16489.6 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G,H

AFTFAAFCYMLALLLTAALIFFAIWHIIAFDELKTDYKNPIDQCNTLNPLVLPEYLIHAFFCVMFLCAAEWLTLGLNMPLLAYHIWRYMSRPVMSGPGLYDPTTIMNADILAYCQKEGWCKLAFYLLAFFYYLYGMIYVLVS

Entity 4 Entity 4 non-polymer

Description description	GLUTAMIC ACID
Molecular weight formula_weight	147.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 non-polymer

Description description	(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
Molecular weight formula_weight	760.1 kDa
Source method src_method	syn
Copy count entity_count	16

Entity 6 Entity 6 non-polymer

Description description	N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dipropane-2-sulfonamide
Molecular weight formula_weight	480.7 kDa
Source method src_method	man
Copy count entity_count	2

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Homo sapiens

Entity 7 Entity 7 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.76 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	76183

fit	/app/data/saxs_computation/ov/9ovv/9ovv.fit
pddf	/app/data/pr_computation/ov/9ovv/9ovv.pr.out
profile	/app/data/saxs_computation/ov/9ovv/9ovv.dat

Heteromeric GluA1/A2-CNIH1 in the activated state, composite map of LBD-TMD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Isoform Flip of Glutamate receptor 1

State in the Current Structure

Other States of the Same Protein in the Database

Isoform Flip of Glutamate receptor 2

State in the Current Structure

Other States of the Same Protein in the Database

Protein cornichon homolog 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

来源 Source

Entity 7 Entity 7 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)