10ff

SK5A-Matured glycine/glutamate in complex with GluN1-GluN2B, full refinement

Method: ELECTRON MICROSCOPY Dmax: 210.5 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–841 Chain C; UniProt 1–841 Not recorded Glutamate receptor ionotropic, NMDA 2B × 2 (Q13224) Light chain × 2 Heavy chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.06 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 1–841; UniProt 1–841 Author chain C; PDBConstruct 1–841; UniProt 1–841

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 27–852 Chain D; UniProt 27–852 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (Q05586) Light chain × 2 Heavy chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.06 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 1–826; UniProt 27–852 Author chain D; PDBConstruct 1–826; UniProt 27–852

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 10ff

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10ff
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10ff
Deposition date deposition_date2026-01-15
Structure title titleSK5A-Matured glycine/glutamate in complex with GluN1-GluN2B, full refinement
Keywords keywordsNMDAR, antibody, SIGNALING PROTEIN, SIGNALING PROTEIN-Immune System complex; SIGNALING PROTEIN/Immune System
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.56
Radius of gyration Rg (electron density) rg_electron60.72
Forward intensity I(0) i01912820000.00
Molecular weight molecular_weight368790.0 kDa
Excluded volume excluded_volume461950 ų
Envelope volume envelope_volume722910 ų
Hydration-shell volume shell_volume105500 ų
Envelope diameter envelope_diameter215.7
Shell Rg shell_rg57.95
Envelope Rg envelope_rg58.66
Shape Rg shape_rg60.72
Total Rg total_rg60.65
Total atoms total_atoms26017
Residues n_residues3535
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 dmax210.5
Rg (real space) rg_real60.60
Rg uncertainty (real space) rg_real_error2.32
I(0) (real space) i0_real1.9130e+09
I(0) uncertainty (real space) i0_real_error4.0350e+07
Rg (reciprocal space) rg_reciprocal60.49
I(0) (reciprocal space) i0_reciprocal1912000000.0000
Solution quality estimate total_estimate0.8705
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.8
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.406
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha114100000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.733

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)