8vhv

Transmembrane AMPA Receptor Regulatory Protein Subunit Gamma 2

Method: ELECTRON MICROSCOPY D_max: 77.6 Å Quality: REASONABLE

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

Voltage-dependent calcium channel gamma-2 subunit

Mus musculus

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–208	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.30 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 8VHV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3JXT Crystal structure of the third PDZ domain of SAP-102 in complex with a fluorogenic peptide-based ligand Deposited 2009-09-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 318–323（6 aa） Fragment：C-terminal motif of Stargazin: UNP O88602 residues 318-323	Mutation：R318(4DB) Non-standard monomer：Yes (specific site not provided by mmCIF)	ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；1.0 M Sodium citrate, 0.1 M Tris-HCl pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.50 Å R-free 0.214
3JXT Crystal structure of the third PDZ domain of SAP-102 in complex with a fluorogenic peptide-based ligand Deposited 2009-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 318–323（6 aa） Fragment：C-terminal motif of Stargazin: UNP O88602 residues 318-323	Mutation：R318(4DB) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；1.0 M Sodium citrate, 0.1 M Tris-HCl pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.50 Å R-free 0.214
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 2–208（207 aa） Chain B 2–208（207 aa） Chain C 2–208（207 aa） Chain D 2–208（207 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 2–208（207 aa） Chain B 2–208（207 aa） Chain C 2–208（207 aa） Chain D 2–208（207 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 2–208（207 aa） Chain B 2–208（207 aa） Chain C 2–208（207 aa） Chain D 2–208（207 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
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 structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–208（207 aa） Fragment：UNP P19491 residues 25-847, UNP O88602 2-208 linked via LINKER GT Chain B 2–208（207 aa） Fragment：UNP P19491 residues 25-847, UNP O88602 2-208 linked via LINKER GT Chain C 2–208（207 aa） Fragment：UNP P19491 residues 25-847, UNP O88602 2-208 linked via LINKER GT Chain D 2–208（207 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
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 aa）	Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E	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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 aa）	Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E	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
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 aa）	Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E	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
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 aa）	Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E	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
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 aa）	Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E	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
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 aa）	Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E	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
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 aa）	Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E	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
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 aa）	Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E Mutation：K52E, K53E	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
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 oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 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 oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 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 oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 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 oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 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 oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 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 oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 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
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 oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa） Chain G 1–323（323 aa） Chain H 1–323（323 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 oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 6–208（203 aa） Chain F 6–208（203 aa） Chain G 6–208（203 aa） Chain H 6–208（203 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 oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 6–208（203 aa） Chain F 6–208（203 aa） Chain G 6–208（203 aa） Chain H 6–208（203 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 oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 6–208（203 aa） Chain F 6–208（203 aa） Chain G 6–208（203 aa） Chain H 6–208（203 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 oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 6–208（203 aa） Chain F 6–208（203 aa） Chain G 6–208（203 aa） Chain H 6–208（203 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 oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 6–208（203 aa） Chain F 6–208（203 aa） Chain G 6–208（203 aa） Chain H 6–208（203 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 oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 3–208（206 aa） Chain F 3–208（206 aa） Chain G 3–208（206 aa） Chain H 3–208（206 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 oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 3–208（206 aa） Chain F 3–208（206 aa） Chain G 3–208（206 aa） Chain H 3–208（206 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
9P9B Activated GluA4 homotetrameric AMPAR. Deposited 2025-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 2–208（207 aa） Chain F 2–208（207 aa） Chain G 2–208（207 aa） Chain H 2–208（207 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.31 Å
9P9C Active substate 1 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 2–208（207 aa） Chain F 2–208（207 aa） Chain G 2–208（207 aa） Chain H 2–208（207 aa）	Not recorded	CYZ CYCLOTHIAZIDE × 4 GLU GLUTAMIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.01 Å
9P9D Active substate 2 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 2–208（207 aa） Chain F 2–208（207 aa） Chain G 2–208（207 aa） Chain H 2–208（207 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.82 Å
9P9E Active substate 3 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 2–208（207 aa） Chain F 2–208（207 aa） Chain G 2–208（207 aa） Chain H 2–208（207 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.82 Å
9P9F Active substate 4 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 2–208（207 aa） Chain F 2–208（207 aa） Chain G 2–208（207 aa） Chain H 2–208（207 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.89 Å
9P9G Active substate 5 of the GluA4 homotetramer. Deposited 2025-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 2–208（207 aa） Chain F 2–208（207 aa） Chain G 2–208（207 aa） Chain H 2–208（207 aa）	Not recorded	GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.06 Å
9ZKM The LBD-TMD structure of native mouse AMPAR with 4 TARPs Deposited 2025-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa）	Not recorded	PLM PALMITIC ACID × 12 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 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 3.13 Å
9ZKN The TMD structure of native mouse AMPAR with 4 TARPs Deposited 2025-12-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–323（323 aa） Chain F 1–323（323 aa）	Not recorded	PLM PALMITIC ACID × 11 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 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 2.80 Å
9ZKQ The LBD-TMD structure of native mouse AMPAR with 3 TARPs 1 CNIH Deposited 2025-12-07	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–323（323 aa）	Not recorded	PLM PALMITIC ACID × 10 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 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 3.36 Å
9ZKR The TMD structure of native mouse AMPAR with 3 TARPs 1 CNIH Deposited 2025-12-07	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–323（323 aa）	Not recorded	PLM PALMITIC ACID × 10 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.08 Å
9ZKU The LBD-TMD structure of native mouse AMPAR with 3 TARPs 1 CNIH and PRRT1/SynDIG4 Deposited 2025-12-07	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain F 1–323（323 aa）	Not recorded	PLM PALMITIC ACID × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 7 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.75 Å
9ZKW The LBD-TMD structure of native mouse AMPAR with 3 TARPs Deposited 2025-12-07	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain E 1–323（323 aa）	Not recorded	PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 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 3.33 Å

39 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CCG2_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–208； UniProt 1–208

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	8vhv
Deposition date deposition_date	2024-01-02
Structure title title	Transmembrane AMPA Receptor Regulatory Protein Subunit Gamma 2
Keywords keywords	tetraspanin, glutamate receptor regulator protein, Claudin-like, 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	20.77 Å
Radius of gyration Rg (electron density) rg_electron	20.01 Å
Forward intensity I(0) i0	5965010.00
Molecular weight molecular_weight	18954.0 kDa
Excluded volume excluded_volume	24234 Å³
Envelope volume envelope_volume	29489 Å³
Hydration-shell volume shell_volume	13687 Å³
Envelope diameter envelope_diameter	76.7 Å
Shell Rg shell_rg	24.55 Å
Envelope Rg envelope_rg	20.84 Å
Shape Rg shape_rg	19.97 Å
Total Rg total_rg	20.93 Å
Total atoms total_atoms	1335
Residues n_residues	172
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	77.6 Å
Rg (real space) rg_real	21.08 Å
Rg uncertainty (real space) rg_real_error	0.92 Å
I(0) (real space) i0_real	5.9650e+06
I(0) uncertainty (real space) i0_real_error	8.5470e+04
Rg (reciprocal space) rg_reciprocal	21.02 Å
I(0) (reciprocal space) i0_reciprocal	5965000.0000
Solution quality estimate total_estimate	0.7291
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.9 Å
Skewness Skewness skewness	0.603
Kurtosis Kurtosis kurtosis	-0.316
Angular range angular_range	— – 0.3850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1759000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.420; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.221; Smooth: 0.992

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (2)

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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	2.30 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	494916

Description description	Voltage-dependent calcium channel gamma-2 subunit
Molecular weight formula_weight	23196.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1335

Transmembrane AMPA Receptor Regulatory Protein Subunit Gamma 2

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

Voltage-dependent calcium channel gamma-2 subunit

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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Homo sapiens

fit	/app/data/saxs_computation/vh/8vhv/8vhv.fit
pddf	/app/data/pr_computation/vh/8vhv/8vhv.pr.out
profile	/app/data/saxs_computation/vh/8vhv/8vhv.dat