8vuh

Human GluN1-2A IgG 003-102 splayed conformation

Method: ELECTRON MICROSCOPY Dmax: 208.3 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 27–841 Chain C; UniProt 26–841 Not recorded Glutamate receptor ionotropic, NMDA 2A × 2 (Q12879) 003-102 Heavy × 2 003-102 Light × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.42 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, 3
Chains and sequence ranges Author chain A; PDBConstruct 1–815; UniProt 27–841 Author chain C; PDBConstruct 1–816; UniProt 26–841

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 34–841 Chain D; UniProt 34–841 Not recorded Glutamate receptor ionotropic, NMDA 1 × 1 (Q05586) Glutamate receptor ionotropic, NMDA 1 × 1 (Q05586) 003-102 Heavy × 2 003-102 Light × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.42 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–808; UniProt 34–841 Author chain D; PDBConstruct 1–808; UniProt 34–841

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 8vuh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vuh
Deposition date deposition_date2024-01-29
Structure title titleHuman GluN1-2A IgG 003-102 splayed conformation
Keywords keywordsReceptor, antibody, ion channel, MEMBRANE-IMMUNE SYSTEM complex; MEMBRANE/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.30
Radius of gyration Rg (electron density) rg_electron60.56
Forward intensity I(0) i01835580000.00
Molecular weight molecular_weight355800.0 kDa
Excluded volume excluded_volume443550 ų
Envelope volume envelope_volume743560 ų
Hydration-shell volume shell_volume107570 ų
Envelope diameter envelope_diameter218.3
Shell Rg shell_rg57.54
Envelope Rg envelope_rg59.47
Shape Rg shape_rg60.62
Total Rg total_rg60.23
Total atoms total_atoms25161
Residues n_residues3587
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 dmax208.3
Rg (real space) rg_real61.35
Rg uncertainty (real space) rg_real_error2.00
I(0) (real space) i0_real1.8360e+09
I(0) uncertainty (real space) i0_real_error4.0250e+07
Rg (reciprocal space) rg_reciprocal61.23
I(0) (reciprocal space) i0_reciprocal1835000000.0000
Solution quality estimate total_estimate0.8808
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.1
Skewness Skewness skewness0.303
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha114600000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.804

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)