8e96

Glycine and glutamate bound Human GluN1a-GluN2D NMDA receptor

Method: ELECTRON MICROSCOPY Dmax: 163.8 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 19–847 Chain C; UniProt 19–847 Mutation:C22S, R844N, R845G, K846A Glutamate receptor ionotropic, NMDA 2D × 2 (O15399) GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 GLU GLUTAMIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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 1–829; UniProt 19–847 Author chain C; PDBConstruct 1–829; UniProt 19–847

Glutamate receptor ionotropic, NMDA 2D

Homo sapiens

UniProt O15399

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 28–879 Chain D; UniProt 28–879 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (Q05586) GLY GLYCINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 GLU GLUTAMIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 36–887; UniProt 28–879 Author chain D; PDBConstruct 36–887; UniProt 28–879

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 8e96

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e96
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e96
Deposition date deposition_date2022-08-26
Structure title titleGlycine and glutamate bound Human GluN1a-GluN2D NMDA receptor
Keywords keywordsLigand-gated ion channel, ionotropic glutamate receptor, synaptic protein, voltage-gate ion channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.53
Radius of gyration Rg (electron density) rg_electron51.09
Forward intensity I(0) i01397570000.00
Molecular weight molecular_weight311040.0 kDa
Excluded volume excluded_volume389400 ų
Envelope volume envelope_volume616010 ų
Hydration-shell volume shell_volume100320 ų
Envelope diameter envelope_diameter174.0
Shell Rg shell_rg55.19
Envelope Rg envelope_rg50.02
Shape Rg shape_rg51.11
Total Rg total_rg51.17
Total atoms total_atoms21924
Residues n_residues2834
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 dmax163.8
Rg (real space) rg_real51.41
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real1.3980e+09
I(0) uncertainty (real space) i0_real_error2.5900e+07
Rg (reciprocal space) rg_reciprocal51.62
I(0) (reciprocal space) i0_reciprocal1398000000.0000
Solution quality estimate total_estimate0.8733
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.4
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.293
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha108800000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.622

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8e96A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id8e96C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)