9pzu

Native GluN1/GluN2B in complex with 5F11 Fab (class 4), glycine and glutamate-bound state

Method: ELECTRON MICROSCOPY Dmax: 195.1 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 × 8 其他Polymer 4 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–938 Chain C; UniProt 1–938 Not recorded Heavy chain of GluN1-specific monoclonal Fab fragment, termed 5F11 × 2 Light chain of GluN1-specific monoclonal Fab fragment, termed 5F11 × 2 Glutamate receptor ionotropic, NMDA 2B × 2 (Q01097) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.36 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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–938; UniProt 1–938 Author chain C; PDBConstruct 1–938; UniProt 1–938

Glutamate receptor ionotropic, NMDA 2B

OrganismNot specified

UniProt Q01097

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 × 8 其他Polymer 4 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–1482 Chain D; UniProt 1–1482 Not recorded Heavy chain of GluN1-specific monoclonal Fab fragment, termed 5F11 × 2 Light chain of GluN1-specific monoclonal Fab fragment, termed 5F11 × 2 Glutamate receptor ionotropic, NMDA 1 × 2 (P35438) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.36 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE2_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–1482; UniProt 1–1482 Author chain D; PDBConstruct 1–1482; UniProt 1–1482

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 9pzu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9pzu
Deposition date deposition_date2025-08-11
Structure title titleNative GluN1/GluN2B in complex with 5F11 Fab (class 4), glycine and glutamate-bound state
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_guinier57.35
Radius of gyration Rg (electron density) rg_electron56.45
Forward intensity I(0) i01443890000.00
Molecular weight molecular_weight313810.0 kDa
Excluded volume excluded_volume390460 ų
Envelope volume envelope_volume653240 ų
Hydration-shell volume shell_volume98653 ų
Envelope diameter envelope_diameter205.3
Shell Rg shell_rg57.84
Envelope Rg envelope_rg54.87
Shape Rg shape_rg56.50
Total Rg total_rg56.30
Total atoms total_atoms22144
Residues n_residues3133
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 dmax195.1
Rg (real space) rg_real57.31
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real1.4440e+09
I(0) uncertainty (real space) i0_real_error2.7860e+07
Rg (reciprocal space) rg_reciprocal57.36
I(0) (reciprocal space) i0_reciprocal1444000000.0000
Solution quality estimate total_estimate0.8755
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.3
Skewness Skewness skewness0.303
Kurtosis Kurtosis kurtosis-0.282
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87340000.0000
Real-space data points n_real_points28
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: 1.000; Smooth: 0.814

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)