8vj7

GluA2 bound to GYKI-52466 and Glutamate, Inhibited State 2

Method: ELECTRON MICROSCOPY Dmax: 200.7 Å Quality: REASONABLE

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

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 25–842 Chain B; UniProt 25–842 Chain C; UniProt 25–842 Chain D; UniProt 25–842 Not recorded GLU GLUTAMIC ACID × 4 A1AB5 4-[(5S,8R)-8-methyl-6,7,8,9-tetrahydro-2H,5H-[1,3]dioxolo[4,5-h][2,3]benzodiazepin-5-yl]aniline × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.85 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–797; UniProt 25–842 Author chain B; PDBConstruct 1–797; UniProt 25–842 Author chain C; PDBConstruct 1–797; UniProt 25–842 Author chain D; PDBConstruct 1–797; UniProt 25–842

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 8vj7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vj7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8vj7
Deposition date deposition_date2024-01-05
Structure title titleGluA2 bound to GYKI-52466 and Glutamate, Inhibited State 2
Keywords keywords;ligand gated ion channel, ionotropic glutamate receptor, allosteric inhibition, MEMBRANE PROTEIN, MEMBRANE PROTEIN-INHIBITOR complex ;; MEMBRANE PROTEIN/INHIBITOR
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.09
Radius of gyration Rg (electron density) rg_electron57.22
Forward intensity I(0) i01720530000.00
Molecular weight molecular_weight357260.0 kDa
Excluded volume excluded_volume451130 ų
Envelope volume envelope_volume652830 ų
Hydration-shell volume shell_volume98527 ų
Envelope diameter envelope_diameter192.2
Shell Rg shell_rg56.77
Envelope Rg envelope_rg55.72
Shape Rg shape_rg57.26
Total Rg total_rg57.04
Total atoms total_atoms25175
Residues n_residues3182
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 dmax200.7
Rg (real space) rg_real57.17
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real1.7210e+09
I(0) uncertainty (real space) i0_real_error3.4420e+07
Rg (reciprocal space) rg_reciprocal57.00
I(0) (reciprocal space) i0_reciprocal1720000000.0000
Solution quality estimate total_estimate0.6284
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.7
Skewness Skewness skewness0.372
Kurtosis Kurtosis kurtosis-0.272
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha119000000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.795; Stabil: 1.000; Sysdev: 0.003; Positv: 1.000; Valcen: 0.995; Smooth: 0.774

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)