7eu8

Structure of the human GluN1-GluN2B NMDA receptor in complex with S-ketamine,glycine and glutamate

Method: ELECTRON MICROSCOPY Dmax: 177.9 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–847 Chain C; UniProt 1–847 Not recorded Glutamate receptor ionotropic, NMDA 2B × 2 (Q13224) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 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 4.07 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.

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 1–847; UniProt 1–847 Author chain C; PDBConstruct 1–847; UniProt 1–847

Glutamate receptor ionotropic, NMDA 2B

Homo sapiens

UniProt Q13224

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 1–842 Chain D; UniProt 1–842 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (Q05586) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 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 4.07 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.

35 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–842; UniProt 1–842 Author chain D; PDBConstruct 1–842; UniProt 1–842

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 7eu8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7eu8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7eu8
Deposition date deposition_date2021-05-16
Structure title titleStructure of the human GluN1-GluN2B NMDA receptor in complex with S-ketamine,glycine and glutamate
Keywords keywordsNMDA receptor, ketamine, enantiomer, rapid antidepressant, cryo-EM structure, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.90
Radius of gyration Rg (electron density) rg_electron51.52
Forward intensity I(0) i01072840000.00
Molecular weight molecular_weight262880.0 kDa
Excluded volume excluded_volume324080 ų
Envelope volume envelope_volume555560 ų
Hydration-shell volume shell_volume92116 ų
Envelope diameter envelope_diameter176.5
Shell Rg shell_rg52.97
Envelope Rg envelope_rg50.40
Shape Rg shape_rg51.57
Total Rg total_rg51.42
Total atoms total_atoms18670
Residues n_residues3010
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 dmax177.9
Rg (real space) rg_real51.86
Rg uncertainty (real space) rg_real_error1.62
I(0) (real space) i0_real1.0730e+09
I(0) uncertainty (real space) i0_real_error2.0760e+07
Rg (reciprocal space) rg_reciprocal51.93
I(0) (reciprocal space) i0_reciprocal1073000000.0000
Solution quality estimate total_estimate0.8757
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.294
Kurtosis Kurtosis kurtosis-0.353
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha101800000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.861

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)