8vvh

rat GluN1a-2B Fab 003-102 local refinement

Method: ELECTRON MICROSCOPY Dmax: 117.9 Å Quality: GOOD

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

Glutamate receptor ionotropic, NMDA 1

Rattus norvegicus

UniProt P35439

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 25–393 Not recorded Glutamate receptor ionotropic, NMDA 2B × 1 (Q00960) 003-102 Heavy × 1 003-102 Light × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.95 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.

114 other PDB entries and 120 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDZ1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–369; UniProt 25–393

Glutamate receptor ionotropic, NMDA 2B

Rattus norvegicus

UniProt Q00960

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 34–387 Not recorded Glutamate receptor ionotropic, NMDA 1 × 1 (P35439) 003-102 Heavy × 1 003-102 Light × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.95 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.

59 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE2_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–354; UniProt 34–387

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 8vvh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vvh
Deposition date deposition_date2024-01-31
Structure title titlerat GluN1a-2B Fab 003-102 local refinement
Keywords keywordsChannel, heterotetramer, receptor, antibody, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.09
Radius of gyration Rg (electron density) rg_electron34.67
Forward intensity I(0) i0149146000.00
Molecular weight molecular_weight97306.0 kDa
Excluded volume excluded_volume121640 ų
Envelope volume envelope_volume172030 ų
Hydration-shell volume shell_volume42540 ų
Envelope diameter envelope_diameter118.8
Shell Rg shell_rg39.93
Envelope Rg envelope_rg34.24
Shape Rg shape_rg34.69
Total Rg total_rg35.00
Total atoms total_atoms6867
Residues n_residues941
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 dmax117.9
Rg (real space) rg_real35.16
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real1.4910e+08
I(0) uncertainty (real space) i0_real_error2.5430e+06
Rg (reciprocal space) rg_reciprocal35.12
I(0) (reciprocal space) i0_reciprocal149100000.0000
Solution quality estimate total_estimate0.8800
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.9
Skewness Skewness skewness0.396
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha82950000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)