9unp

native NMDA receptor-GluN1/N2A/N2B-S2 in the closed state

Method: ELECTRON MICROSCOPY Dmax: 181.0 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 24–844 Chain C; UniProt 24–844 Not recorded Glutamate receptor ionotropic, NMDA 2A × 1 (P35436) Glutamate receptor ionotropic, NMDA 2B × 1 (Q01097) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 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 3.27 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 1–821; UniProt 24–844 Author chain C; PDBConstruct 1–821; UniProt 24–844

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 35–839 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (P35438) Glutamate receptor ionotropic, NMDA 2B × 1 (Q01097) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 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 3.27 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 1–805; UniProt 35–839

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 32–842 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (P35438) Glutamate receptor ionotropic, NMDA 2A × 1 (P35436) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 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 3.27 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 1–811; UniProt 32–842

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 9unp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9unp
Deposition date deposition_date2025-04-24
Structure title titlenative NMDA receptor-GluN1/N2A/N2B-S2 in the closed state
Keywords keywordsnative, NMDA receptor, inotropic ion channel, excitatory neurotransmitter, MEMBRANE, open state, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.60
Radius of gyration Rg (electron density) rg_electron52.56
Forward intensity I(0) i01503820000.00
Molecular weight molecular_weight328920.0 kDa
Excluded volume excluded_volume413590 ų
Envelope volume envelope_volume611960 ų
Hydration-shell volume shell_volume98941 ų
Envelope diameter envelope_diameter180.4
Shell Rg shell_rg54.28
Envelope Rg envelope_rg51.44
Shape Rg shape_rg52.56
Total Rg total_rg52.64
Total atoms total_atoms23173
Residues n_residues3142
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 dmax181.0
Rg (real space) rg_real52.55
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real1.5040e+09
I(0) uncertainty (real space) i0_real_error2.9170e+07
Rg (reciprocal space) rg_reciprocal52.62
I(0) (reciprocal space) i0_reciprocal1504000000.0000
Solution quality estimate total_estimate0.8712
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.4
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.310
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha113200000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.847

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)