7eot

Structure of the human GluN1/GluN2A NMDA receptor in the CGP-78608/glutamate bound state

Method: ELECTRON MICROSCOPY Dmax: 183.9 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 J86 [(1S)-1-[[7-bromanyl-2,3-bis(oxidanylidene)-1,4-dihydroquinoxalin-5-yl]methylamino]ethyl]phosphonic acid × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 J86 [(1S)-1-[[7-bromanyl-2,3-bis(oxidanylidene)-1,4-dihydroquinoxalin-5-yl]methylamino]ethyl]phosphonic acid × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 7eot

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7eot
Deposition date deposition_date2021-04-22
Structure title titleStructure of the human GluN1/GluN2A NMDA receptor in the CGP-78608/glutamate 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_guinier52.98
Radius of gyration Rg (electron density) rg_electron53.39
Forward intensity I(0) i01688730000.00
Molecular weight molecular_weight349700.0 kDa
Excluded volume excluded_volume440330 ų
Envelope volume envelope_volume664340 ų
Hydration-shell volume shell_volume104430 ų
Envelope diameter envelope_diameter186.0
Shell Rg shell_rg55.37
Envelope Rg envelope_rg53.10
Shape Rg shape_rg53.39
Total Rg total_rg53.44
Total atoms total_atoms24620
Residues n_residues3088
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 dmax183.9
Rg (real space) rg_real52.97
Rg uncertainty (real space) rg_real_error1.76
I(0) (real space) i0_real1.6890e+09
I(0) uncertainty (real space) i0_real_error3.5750e+07
Rg (reciprocal space) rg_reciprocal52.97
I(0) (reciprocal space) i0_reciprocal1689000000.0000
Solution quality estimate total_estimate0.8625
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.3
Skewness Skewness skewness0.360
Kurtosis Kurtosis kurtosis-0.231
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha233300000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.808

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)