Current Protein Identity:O88602 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method 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 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
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 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
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 Assembly 1 Insufficient information Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
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 Assembly 1 Insufficient information Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
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 Assembly 1 Insufficient information Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
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 Assembly 1 Insufficient information Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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
8VHV Transmembrane AMPA Receptor Regulatory Protein Subunit Gamma 2 Deposited 2024-01-02 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–208(208 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.30 Å
9B5Z GluA2 flip Q in complex with TARPgamma2 at pH8, consensus structure of LBD-TMD-TARPgamma2 Deposited 2024-03-23 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 9 PDB declaration: nonameric(9) Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer;Protein × 7 PDB declaration: heptameric(7) Consistent with protein count
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