9pzv

Native GluN1/GluN2A in complex with 5F11 and 3D2 Fabs, local ATD dimer

Method: ELECTRON MICROSCOPY Dmax: 123.9 Å Quality: GOOD

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

Glutamate receptor ionotropic, NMDA 1

OrganismNot specified

UniProt P35438

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–938 Not recorded Glutamate receptor ionotropic, NMDA 2A × 1 (P35436) Heavy chain of GluN1-specific monoclonal Fab fragment, termed 5F11 × 1 Light chain of GluN1-specific monoclonal Fab fragment, termed 5F11 × 1 Heavy chain of GluN2A-specific monoclonal Fab fragment, termed 3D2 × 1 Light chain of GluN2A-specific monoclonal Fab fragment, termed 3D2 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.92 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDZ1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–938; UniProt 1–938

Glutamate receptor ionotropic, NMDA 2A

OrganismNot specified

UniProt P35436

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–1464 Not recorded Glutamate receptor ionotropic, NMDA 1 × 1 (P35438) Heavy chain of GluN1-specific monoclonal Fab fragment, termed 5F11 × 1 Light chain of GluN1-specific monoclonal Fab fragment, termed 5F11 × 1 Heavy chain of GluN2A-specific monoclonal Fab fragment, termed 3D2 × 1 Light chain of GluN2A-specific monoclonal Fab fragment, termed 3D2 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.92 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1464; UniProt 1–1464

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 9pzv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pzv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pzv
Deposition date deposition_date2025-08-11
Structure title titleNative GluN1/GluN2A in complex with 5F11 and 3D2 Fabs, local ATD dimer
Keywords keywordsligand-gated ion channel, NMDA, antibody, native, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.84
Radius of gyration Rg (electron density) rg_electron37.26
Forward intensity I(0) i0210877000.00
Molecular weight molecular_weight113970.0 kDa
Excluded volume excluded_volume141090 ų
Envelope volume envelope_volume211140 ų
Hydration-shell volume shell_volume48204 ų
Envelope diameter envelope_diameter131.7
Shell Rg shell_rg42.29
Envelope Rg envelope_rg36.81
Shape Rg shape_rg37.30
Total Rg total_rg37.52
Total atoms total_atoms8069
Residues n_residues1145
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 dmax123.9
Rg (real space) rg_real37.81
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real2.1090e+08
I(0) uncertainty (real space) i0_real_error3.3200e+06
Rg (reciprocal space) rg_reciprocal37.83
I(0) (reciprocal space) i0_reciprocal210900000.0000
Solution quality estimate total_estimate0.8961
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.2
Skewness Skewness skewness0.263
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50230000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.885

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)