9ovt

Heteromeric GluA1/A2 in the inactive state, composite map of LBD-TMD

Method: ELECTRON MICROSCOPY Dmax: 137.2 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 403–833 Chain C; UniProt 403–833 Not recorded Glutamate receptor 2 × 2 (P19491) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NA SODIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 100 uM ZK-200775 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.43 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 1–431; UniProt 403–833 Author chain C; PDBConstruct 1–431; UniProt 403–833

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 413–841 Chain D; UniProt 413–841 Not recorded Glutamate receptor 1 × 2 (P19490) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NA SODIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 100 uM ZK-200775 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.43 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
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–429; UniProt 413–841 Author chain D; PDBConstruct 1–429; UniProt 413–841

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 9ovt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ovt
Deposition date deposition_date2025-05-31
Structure title titleHeteromeric GluA1/A2 in the inactive state, composite map of LBD-TMD
Keywords keywordsGluA1A2 heterotetramer ZK iGluR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.76
Radius of gyration Rg (electron density) rg_electron41.53
Forward intensity I(0) i0466437000.00
Molecular weight molecular_weight184910.0 kDa
Excluded volume excluded_volume234730 ų
Envelope volume envelope_volume321940 ų
Hydration-shell volume shell_volume64799 ų
Envelope diameter envelope_diameter140.9
Shell Rg shell_rg46.38
Envelope Rg envelope_rg41.14
Shape Rg shape_rg41.58
Total Rg total_rg41.64
Total atoms total_atoms13003
Residues n_residues1648
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 dmax137.2
Rg (real space) rg_real41.70
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real4.6640e+08
I(0) uncertainty (real space) i0_real_error7.4010e+06
Rg (reciprocal space) rg_reciprocal41.76
I(0) (reciprocal space) i0_reciprocal466500000.0000
Solution quality estimate total_estimate0.8965
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.3
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis-0.583
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha119400000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)