9qpw

GluA4, resting state, structure of TMD/LBD

Method: ELECTRON MICROSCOPY Dmax: 124.0 Å Quality: GOOD

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

Isoform 2 of Glutamate receptor 4

Rattus norvegicus

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 21–902 Chain B; UniProt 21–902 Chain C; UniProt 21–902 Chain D; UniProt 21–902 Not recorded E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–882; UniProt 21–902 Author chain B; PDBConstruct 1–882; UniProt 21–902 Author chain C; PDBConstruct 1–882; UniProt 21–902 Author chain D; PDBConstruct 1–882; UniProt 21–902

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 9qpw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qpw
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9qpw
Deposition date deposition_date2025-03-29
Structure title titleGluA4, resting state, structure of TMD/LBD
Keywords keywordsGluA4, GRIA4, TMD/LBD, Resting state, NBQX, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.36
Radius of gyration Rg (electron density) rg_electron40.28
Forward intensity I(0) i0388767000.00
Molecular weight molecular_weight170700.0 kDa
Excluded volume excluded_volume217620 ų
Envelope volume envelope_volume298500 ų
Hydration-shell volume shell_volume61458 ų
Envelope diameter envelope_diameter127.6
Shell Rg shell_rg46.12
Envelope Rg envelope_rg39.49
Shape Rg shape_rg40.30
Total Rg total_rg40.58
Total atoms total_atoms12012
Residues n_residues1534
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 dmax124.0
Rg (real space) rg_real40.24
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real3.8880e+08
I(0) uncertainty (real space) i0_real_error5.9140e+06
Rg (reciprocal space) rg_reciprocal40.36
I(0) (reciprocal space) i0_reciprocal388800000.0000
Solution quality estimate total_estimate0.8979
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.5
Skewness Skewness skewness0.128
Kurtosis Kurtosis kurtosis-0.684
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha98200000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.769

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)