9mum

Crystal structure of GluN1/GluN2A ligand-binding domain in complex with Compound 11, Glycine and Glutamate

Method: X-RAY DIFFRACTION Dmax: 84.3 Å Quality: GOOD

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

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 A; UniProt 394–544 Chain A; UniProt 663–800 Not recorded Glutamate receptor ionotropic, NMDA 2A × 1 (Q12879) GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1 A1BRB 5-[2-(3-chlorophenyl)-2,2-difluoroethoxy]-N-[1-(pyrazin-2-yl)cyclopropyl]pyrazine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.1M Hepes pH 7.0, 0.2M ammonium acetate, 20% PEG-3350 Resolution 1.97 Å R-free 0.241

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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 16–166; UniProt 394–544 Author chain A; PDBConstruct 169–306; UniProt 663–800

Glutamate receptor ionotropic, NMDA 2A

Homo sapiens

UniProt Q12879

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 401–539 Chain B; UniProt 661–802 Not recorded Glutamate receptor ionotropic, NMDA 1 × 1 (Q05586) GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1 A1BRB 5-[2-(3-chlorophenyl)-2,2-difluoroethoxy]-N-[1-(pyrazin-2-yl)cyclopropyl]pyrazine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.1M Hepes pH 7.0, 0.2M ammonium acetate, 20% PEG-3350 Resolution 1.97 Å R-free 0.241

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.

35 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 15–153; UniProt 401–539 Author chain B; PDBConstruct 156–297; UniProt 661–802

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 9mum

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mum
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9mum
Deposition date deposition_date2025-01-14
Structure title titleCrystal structure of GluN1/GluN2A ligand-binding domain in complex with Compound 11, Glycine and Glutamate
Keywords keywordsNMDARS, LBD, ION CHANNELS, METAL TRANSPORT, NEGATIVE MODULATOR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.38
Radius of gyration Rg (electron density) rg_electron24.44
Forward intensity I(0) i0118588000.00
Molecular weight molecular_weight57396.0 kDa
Excluded volume excluded_volume55522 ų
Envelope volume envelope_volume93023 ų
Hydration-shell volume shell_volume31072 ų
Envelope diameter envelope_diameter88.4
Shell Rg shell_rg32.32
Envelope Rg envelope_rg24.77
Shape Rg shape_rg24.41
Total Rg total_rg25.12
Total atoms total_atoms4339
Residues n_residues548
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 dmax84.3
Rg (real space) rg_real25.29
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real1.1860e+08
I(0) uncertainty (real space) i0_real_error1.8890e+06
Rg (reciprocal space) rg_reciprocal25.32
I(0) (reciprocal space) i0_reciprocal118600000.0000
Solution quality estimate total_estimate0.8848
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.8
Skewness Skewness skewness0.252
Kurtosis Kurtosis kurtosis-0.317
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18660000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)