7teq

Cryo-EM structure of GluN1b-2B NMDAR in complex with Fab5 active conformation

Method: ELECTRON MICROSCOPY Dmax: 199.6 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–859 Chain C; UniProt 1–859 Not recorded Glutamate receptor ionotropic, NMDA 2B × 2 (Q00960) Fab5 heavy chain × 2 Fab5 light chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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 P35439-7
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–859; UniProt 1–859 Author chain C; PDBConstruct 1–859; UniProt 1–859

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 × 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 (P35439) Fab5 heavy chain × 2 Fab5 light chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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 58–883; UniProt 27–852 Author chain D; PDBConstruct 58–883; 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 7teq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7teq
Deposition date deposition_date2022-01-05
Structure title titleCryo-EM structure of GluN1b-2B NMDAR in complex with Fab5 active conformation
Keywords keywordschannel, antibody, 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_guinier58.72
Radius of gyration Rg (electron density) rg_electron58.94
Forward intensity I(0) i02044860000.00
Molecular weight molecular_weight385760.0 kDa
Excluded volume excluded_volume485630 ų
Envelope volume envelope_volume775740 ų
Hydration-shell volume shell_volume113260 ų
Envelope diameter envelope_diameter201.3
Shell Rg shell_rg58.06
Envelope Rg envelope_rg57.44
Shape Rg shape_rg58.95
Total Rg total_rg58.88
Total atoms total_atoms27140
Residues n_residues3442
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 dmax199.6
Rg (real space) rg_real58.66
Rg uncertainty (real space) rg_real_error1.81
I(0) (real space) i0_real2.0450e+09
I(0) uncertainty (real space) i0_real_error4.2210e+07
Rg (reciprocal space) rg_reciprocal58.73
I(0) (reciprocal space) i0_reciprocal2045000000.0000
Solution quality estimate total_estimate0.8817
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.5
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha139500000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.846

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)