7eou

Structure of the human GluN1/GluN2A NMDA receptor in the glycine/glutamate/GNE-6901/9-AA bound state

Method: ELECTRON MICROSCOPY Dmax: 181.3 Å Quality: GOOD

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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–842 Chain C; UniProt 1–842 Mutation:L794C Glutamate receptor ionotropic, NMDA 1 × 2 (Q05586) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 AA 9-AMINOACRIDINE × 1 6RM 7-[(4-fluoranylphenoxy)methyl]-3-[(1~{R},2~{R})-2-(hydroxymethyl)cyclopropyl]-2-methyl-[1,3]thiazolo[3,2-a]pyrimidin-5-one × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–842; UniProt 1–842 Author chain C; PDBConstruct 1–842; UniProt 1–842

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 B; UniProt 1–847 Chain D; UniProt 1–847 Mutation:E698C Glutamate receptor ionotropic, NMDA 2A × 2 (Q12879) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 AA 9-AMINOACRIDINE × 1 6RM 7-[(4-fluoranylphenoxy)methyl]-3-[(1~{R},2~{R})-2-(hydroxymethyl)cyclopropyl]-2-methyl-[1,3]thiazolo[3,2-a]pyrimidin-5-one × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–847; UniProt 1–847 Author chain D; PDBConstruct 1–847; UniProt 1–847

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 7eou

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7eou
Deposition date deposition_date2021-04-22
Structure title titleStructure of the human GluN1/GluN2A NMDA receptor in the glycine/glutamate/GNE-6901/9-AA bound state
Keywords keywordsNMDA receptor, 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_electron52.92
Forward intensity I(0) i01679240000.00
Molecular weight molecular_weight349460.0 kDa
Excluded volume excluded_volume440370 ų
Envelope volume envelope_volume661700 ų
Hydration-shell volume shell_volume104920 ų
Envelope diameter envelope_diameter183.5
Shell Rg shell_rg55.29
Envelope Rg envelope_rg52.33
Shape Rg shape_rg52.92
Total Rg total_rg53.00
Total atoms total_atoms24631
Residues n_residues3084
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 dmax181.3
Rg (real space) rg_real52.57
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real1.6790e+09
I(0) uncertainty (real space) i0_real_error3.7130e+07
Rg (reciprocal space) rg_reciprocal52.62
I(0) (reciprocal space) i0_reciprocal1679000000.0000
Solution quality estimate total_estimate0.8643
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.4
Skewness Skewness skewness0.341
Kurtosis Kurtosis kurtosis-0.242
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha192000000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.812

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)