9unr

native NMDA receptor-GluN1/N2A/N2B-S1 in the closed state

Method: ELECTRON MICROSCOPY Dmax: 180.8 Å Quality: GOOD

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

Glutamate receptor ionotropic, NMDA 1

OrganismNot specified

UniProt P35438

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 25–843 Chain C; UniProt 25–843 Not recorded Glutamate receptor ionotropic, NMDA 2A × 1 (P35436) Glutamate receptor ionotropic, NMDA 2B × 1 (Q01097) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2 JC9 (2~{S})-2-(2-chlorophenyl)-2-(methylamino)cyclohexan-1-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDZ1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–819; UniProt 25–843 Author chain C; PDBConstruct 1–819; UniProt 25–843

Glutamate receptor ionotropic, NMDA 2A

OrganismNot specified

UniProt P35436

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 33–841 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (P35438) Glutamate receptor ionotropic, NMDA 2B × 1 (Q01097) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2 JC9 (2~{S})-2-(2-chlorophenyl)-2-(methylamino)cyclohexan-1-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–809; UniProt 33–841

Glutamate receptor ionotropic, NMDA 2B

OrganismNot specified

UniProt Q01097

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 D; UniProt 34–841 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (P35438) Glutamate receptor ionotropic, NMDA 2A × 1 (P35436) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19 GLY GLYCINE × 2 GLU GLUTAMIC ACID × 2 JC9 (2~{S})-2-(2-chlorophenyl)-2-(methylamino)cyclohexan-1-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE2_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–808; UniProt 34–841

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 9unr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9unr
Deposition date deposition_date2025-04-24
Structure title titlenative NMDA receptor-GluN1/N2A/N2B-S1 in the closed state
Keywords keywordsnative, NMDA receptor, ionotropic ion channel, excitatory neurotransmitter, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.12
Radius of gyration Rg (electron density) rg_electron53.19
Forward intensity I(0) i01594000000.00
Molecular weight molecular_weight339920.0 kDa
Excluded volume excluded_volume427920 ų
Envelope volume envelope_volume621600 ų
Hydration-shell volume shell_volume99408 ų
Envelope diameter envelope_diameter181.3
Shell Rg shell_rg54.81
Envelope Rg envelope_rg51.86
Shape Rg shape_rg53.19
Total Rg total_rg53.24
Total atoms total_atoms23939
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 dmax180.8
Rg (real space) rg_real53.05
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real1.5940e+09
I(0) uncertainty (real space) i0_real_error3.2210e+07
Rg (reciprocal space) rg_reciprocal53.17
I(0) (reciprocal space) i0_reciprocal1594000000.0000
Solution quality estimate total_estimate0.8124
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.3
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.377
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha115700000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)