6qkc

GluA1/2 In complex with auxiliary subunit gamma-8

Method: ELECTRON MICROSCOPY Dmax: 132.1 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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–907 Chain C; UniProt 1–907 Not recorded Glutamate receptor 2 × 2 (P19491) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW5) E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;25 mM TRIS, pH 8, 150 mM NaCl and 0.1 % digitonin (w/v) cryo-EM vitrification conditions:Cryogen ETHANE;3uL on grid, 60 sec incubation and 4sec blotting time Resolution 4.40 Å

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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–860 Chain D; UniProt 1–860 Not recorded Glutamate receptor 1 × 2 (P19490) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW5) E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;25 mM TRIS, pH 8, 150 mM NaCl and 0.1 % digitonin (w/v) cryo-EM vitrification conditions:Cryogen ETHANE;3uL on grid, 60 sec incubation and 4sec blotting time Resolution 4.40 Å

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

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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) 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) E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;25 mM TRIS, pH 8, 150 mM NaCl and 0.1 % digitonin (w/v) cryo-EM vitrification conditions:Cryogen ETHANE;3uL on grid, 60 sec incubation and 4sec blotting time Resolution 4.40 Å

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 3
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 6qkc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6qkc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6qkc
Deposition date deposition_date2019-01-28
Structure title titleGluA1/2 In complex with auxiliary subunit gamma-8
Keywords keywordsAMPAR, ion channel, GluA1, GluA2, tarp, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.58
Radius of gyration Rg (electron density) rg_electron44.02
Forward intensity I(0) i0488188000.00
Molecular weight molecular_weight195060.0 kDa
Excluded volume excluded_volume249370 ų
Envelope volume envelope_volume380260 ų
Hydration-shell volume shell_volume71648 ų
Envelope diameter envelope_diameter140.0
Shell Rg shell_rg49.34
Envelope Rg envelope_rg42.79
Shape Rg shape_rg44.04
Total Rg total_rg44.21
Total atoms total_atoms13794
Residues n_residues1902
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 dmax132.1
Rg (real space) rg_real44.38
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real4.8820e+08
I(0) uncertainty (real space) i0_real_error8.3100e+06
Rg (reciprocal space) rg_reciprocal44.58
I(0) (reciprocal space) i0_reciprocal488300000.0000
Solution quality estimate total_estimate0.8714
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.4
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.640
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha92660000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.983; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.386

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)