Current Protein Identity:O88602
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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 |