9nra

The structure of GluA1/A4 LBD-TMD with 4 auxiliary subunits

Method: ELECTRON MICROSCOPY Dmax: 145.1 Å Quality: GOOD

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

Glutamate receptor 1

OrganismNot specified

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 407–833 Chain C; UniProt 407–833 Not recorded Isoform 2 of Glutamate receptor 4 × 2 (P19493) ;Auxiliary protein at A'/C' ; × 2 Voltage-dependent calcium channel gamma-2 subunit × 2 (Q71RJ2) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–427; UniProt 407–833 Author chain C; PDBConstruct 1–427; UniProt 407–833

Isoform 2 of Glutamate receptor 4

OrganismNot specified

UniProt P19493

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 417–840 Chain D; UniProt 417–840 Not recorded Glutamate receptor 1 × 2 (P19490) ;Auxiliary protein at A'/C' ; × 2 Voltage-dependent calcium channel gamma-2 subunit × 2 (Q71RJ2) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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.

25 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA4_RAT
Isoform P19493-2
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–424; UniProt 417–840 Author chain D; PDBConstruct 1–424; UniProt 417–840

Voltage-dependent calcium channel gamma-2 subunit

OrganismNot specified

UniProt Q71RJ2

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 5–208 Chain H; UniProt 5–208 Not recorded Glutamate receptor 1 × 2 (P19490) Isoform 2 of Glutamate receptor 4 × 2 (P19493) ;Auxiliary protein at A'/C' ; × 2 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG2_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–204; UniProt 5–208 Author chain H; PDBConstruct 1–204; UniProt 5–208

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

SAXS profile for 9nra

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9nra
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9nra
Deposition date deposition_date2025-03-14
Structure title titleThe structure of GluA1/A4 LBD-TMD with 4 auxiliary subunits
Keywords keywordsiGluR, CP-AMPA receptors, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.97
Radius of gyration Rg (electron density) rg_electron44.38
Forward intensity I(0) i0688622000.00
Molecular weight molecular_weight221060.0 kDa
Excluded volume excluded_volume277960 ų
Envelope volume envelope_volume415920 ų
Hydration-shell volume shell_volume76945 ų
Envelope diameter envelope_diameter146.2
Shell Rg shell_rg50.14
Envelope Rg envelope_rg43.37
Shape Rg shape_rg44.39
Total Rg total_rg44.60
Total atoms total_atoms15598
Residues n_residues2195
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 dmax145.1
Rg (real space) rg_real44.74
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real6.8860e+08
I(0) uncertainty (real space) i0_real_error1.0900e+07
Rg (reciprocal space) rg_reciprocal44.97
I(0) (reciprocal space) i0_reciprocal688800000.0000
Solution quality estimate total_estimate0.8973
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary58.0
Skewness Skewness skewness0.119
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha93910000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)