9gig

NMDA bound to compound 387

Method: X-RAY DIFFRACTION Dmax: 86.2 Å Quality: GOOD

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

Glutamate receptor

Rattus norvegicus

UniProt G3V9C5

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 401–539 Chain A; UniProt 661–802 Not recorded Isoform 1 of Glutamate receptor ionotropic, NMDA 1 × 1 (Q05586) GLU GLUTAMIC ACID × 1 A1ILO (2~{R})-2-azanyl-3-[[3-(5-ethyl-3-methyl-1,2-oxazol-4-yl)-5-fluoranyl-phenyl]carbonylamino]propanoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;282.15 K;10-15% PEG 3350, 0.1 M HEPES pH 7.0, 1 mM sodium azide, 1% tryptone Resolution 2.09 Å R-free 0.257

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G3V9C5_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–141; UniProt 401–539 Author chain A; PDBConstruct 144–285; UniProt 661–802

Isoform 1 of Glutamate receptor ionotropic, NMDA 1

Homo sapiens

UniProt Q05586

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 394–544 Chain B; UniProt 663–800 Not recorded Glutamate receptor × 1 (G3V9C5) GLU GLUTAMIC ACID × 1 A1ILO (2~{R})-2-azanyl-3-[[3-(5-ethyl-3-methyl-1,2-oxazol-4-yl)-5-fluoranyl-phenyl]carbonylamino]propanoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;282.15 K;10-15% PEG 3350, 0.1 M HEPES pH 7.0, 1 mM sodium azide, 1% tryptone Resolution 2.09 Å R-free 0.257

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.

83 other PDB entries and 86 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDZ1_HUMAN
Isoform Q05586-2
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–151; UniProt 394–544 Author chain B; PDBConstruct 154–291; UniProt 663–800

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 9gig

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9gig
Deposition date deposition_date2024-08-19
Structure title titleNMDA bound to compound 387
Keywords keywordsion transport ligand gated ion channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.10
Radius of gyration Rg (electron density) rg_electron24.80
Forward intensity I(0) i060172400.00
Molecular weight molecular_weight61308.0 kDa
Excluded volume excluded_volume77081 ų
Envelope volume envelope_volume94233 ų
Hydration-shell volume shell_volume31150 ų
Envelope diameter envelope_diameter89.6
Shell Rg shell_rg32.54
Envelope Rg envelope_rg25.01
Shape Rg shape_rg24.75
Total Rg total_rg25.83
Total atoms total_atoms8573
Residues n_residues550
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 dmax86.2
Rg (real space) rg_real26.00
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real6.0170e+07
I(0) uncertainty (real space) i0_real_error7.4990e+05
Rg (reciprocal space) rg_reciprocal26.03
I(0) (reciprocal space) i0_reciprocal60170000.0000
Solution quality estimate total_estimate0.8884
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.5
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12500000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)