9ovw

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

Method: ELECTRON MICROSCOPY Dmax: 199.2 Å Quality: GOOD

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

Isoform Flip of 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 23–833 Chain C; UniProt 23–833 Not recorded Isoform Flip of Glutamate receptor 2 × 2 (P19491) QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 1 mM quiqualate cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.91 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 1–805; UniProt 23–833 Author chain C; PDBConstruct 1–805; UniProt 23–833

Isoform Flip of 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 25–841 Chain D; UniProt 25–841 Not recorded Isoform Flip of Glutamate receptor 1 × 2 (P19490) QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;150 mM NaCl, 20 mM Tris-HCl pH 8.0, and 0.05% digitonin, 1 mM quiqualate cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.91 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 1–811; UniProt 25–841 Author chain D; PDBConstruct 1–811; UniProt 25–841

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 9ovw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ovw
Deposition date deposition_date2025-05-31
Structure title titleHeteromeric GluA1/A2 in the desensitized state, composite map of ATD-LBD-TMD
Keywords keywordsGluA1A2 heterotetramer quisqualate 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_guinier56.45
Radius of gyration Rg (electron density) rg_electron56.68
Forward intensity I(0) i01694120000.00
Molecular weight molecular_weight353850.0 kDa
Excluded volume excluded_volume446640 ų
Envelope volume envelope_volume649790 ų
Hydration-shell volume shell_volume98063 ų
Envelope diameter envelope_diameter194.0
Shell Rg shell_rg56.63
Envelope Rg envelope_rg56.00
Shape Rg shape_rg56.73
Total Rg total_rg56.52
Total atoms total_atoms24938
Residues n_residues3154
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 dmax199.2
Rg (real space) rg_real56.53
Rg uncertainty (real space) rg_real_error2.07
I(0) (real space) i0_real1.6940e+09
I(0) uncertainty (real space) i0_real_error3.3510e+07
Rg (reciprocal space) rg_reciprocal56.36
I(0) (reciprocal space) i0_reciprocal1694000000.0000
Solution quality estimate total_estimate0.8569
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.2
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.255
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha116700000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.785; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.785

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)