7oca

Resting state full-length GluA1/A2 heterotertramer in complex with TARP gamma 8 and CNIH2

Method: ELECTRON MICROSCOPY Dmax: 246.4 Å Quality: GOOD

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

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 Other combination Heteromer Protein × 8 其他Polymer 6 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–907 Chain C; UniProt 1–907 Not recorded Glutamate receptor 2 × 2 (P19491) Protein cornichon homolog 2 × 2 (Q5BJU5) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW5) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 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

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.

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 1–915; UniProt 1–907 Author chain C; PDBConstruct 1–915; UniProt 1–907

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 Other combination Heteromer Protein × 8 其他Polymer 6 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–860 Chain D; UniProt 1–860 Not recorded Glutamate receptor 1 × 2 (P19490) Protein cornichon homolog 2 × 2 (Q5BJU5) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW5) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 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

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.

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 1–860; UniProt 1–860 Author chain D; PDBConstruct 1–860; UniProt 1–860

Protein cornichon homolog 2

Rattus norvegicus

UniProt Q5BJU5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 8 其他Polymer 6 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–160 Chain G; UniProt 1–160 Not recorded Glutamate receptor 1 × 2 (P19490) Glutamate receptor 2 × 2 (P19491) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW5) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 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

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNIH2_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–160; UniProt 1–160 Author chain G; PDBConstruct 1–160; UniProt 1–160

Voltage-dependent calcium channel gamma-8 subunit

Rattus norvegicus

UniProt Q8VHW5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 8 其他Polymer 6 PDB declaration: octameric(8) Consistent with protein copy count Chain I; UniProt 2–417 Chain J; UniProt 2–417 Not recorded Glutamate receptor 1 × 2 (P19490) Glutamate receptor 2 × 2 (P19491) Protein cornichon homolog 2 × 2 (Q5BJU5) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 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

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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG8_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain I; PDBConstruct 2–417; UniProt 2–417 Author chain J; PDBConstruct 2–417; UniProt 2–417

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

SAXS profile for 7oca

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7oca
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7oca
Deposition date deposition_date2021-04-26
Structure title titleResting state full-length GluA1/A2 heterotertramer in complex with TARP gamma 8 and CNIH2
Keywords keywordsAMPAR, ion channels, neurotransmission, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.53
Radius of gyration Rg (electron density) rg_electron68.14
Forward intensity I(0) i02081820000.00
Molecular weight molecular_weight414530.0 kDa
Excluded volume excluded_volume530460 ų
Envelope volume envelope_volume825450 ų
Hydration-shell volume shell_volume108130 ų
Envelope diameter envelope_diameter229.9
Shell Rg shell_rg60.44
Envelope Rg envelope_rg65.65
Shape Rg shape_rg68.16
Total Rg total_rg67.88
Total atoms total_atoms29294
Residues n_residues3802
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax246.4
Rg (real space) rg_real67.74
Rg uncertainty (real space) rg_real_error2.73
I(0) (real space) i0_real2.0820e+09
I(0) uncertainty (real space) i0_real_error4.3850e+07
Rg (reciprocal space) rg_reciprocal66.74
I(0) (reciprocal space) i0_reciprocal2078000000.0000
Solution quality estimate total_estimate0.8402
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.0
Skewness Skewness skewness0.415
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0013
Highest regularization parameter α highest_alpha96840000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.719; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.926; Smooth: 0.835

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7ocaI01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily150
Domain ID domain_id7ocaJ01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily150

8. Citations (1)

9. Files and Curves (10)