9oot

Pre-active state of Gly/Glu/Pregnenolone Sulfate bound hGluN1a-2B NMDAR

Method: ELECTRON MICROSCOPY Dmax: 184.8 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 18–847 Chain C; UniProt 18–847 Mutation:C22S,R844N,R845G,K846A Glutamate receptor ionotropic, NMDA 2B × 2 (Q13224) GLY GLYCINE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4 GLU GLUTAMIC ACID × 2 A8W Pregnenolone sulfate × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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
Chains and sequence ranges Author chain A; PDBConstruct 1–830; UniProt 18–847 Author chain C; PDBConstruct 1–830; UniProt 18–847

Glutamate receptor ionotropic, NMDA 2B

Homo sapiens

UniProt Q13224

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 27–852 Chain D; UniProt 27–852 Mutation:C588S,C838S,C849S Glutamate receptor ionotropic, NMDA 1 × 2 (Q05586) GLY GLYCINE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 4 GLU GLUTAMIC ACID × 2 A8W Pregnenolone sulfate × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 36–861; UniProt 27–852 Author chain D; PDBConstruct 36–861; 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 9oot

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9oot
Deposition date deposition_date2025-05-16
Structure title titlePre-active state of Gly/Glu/Pregnenolone Sulfate bound hGluN1a-2B NMDAR
Keywords keywordsN-methyl-D-aspartate receptor, pre-active, GluN2B, Pregnenolone Sulfate, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.91
Radius of gyration Rg (electron density) rg_electron54.42
Forward intensity I(0) i01671450000.00
Molecular weight molecular_weight352720.0 kDa
Excluded volume excluded_volume445870 ų
Envelope volume envelope_volume634530 ų
Hydration-shell volume shell_volume100130 ų
Envelope diameter envelope_diameter183.5
Shell Rg shell_rg54.64
Envelope Rg envelope_rg53.34
Shape Rg shape_rg54.42
Total Rg total_rg54.43
Total atoms total_atoms24825
Residues n_residues3150
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 dmax184.8
Rg (real space) rg_real53.92
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real1.6710e+09
I(0) uncertainty (real space) i0_real_error3.1880e+07
Rg (reciprocal space) rg_reciprocal53.89
I(0) (reciprocal space) i0_reciprocal1671000000.0000
Solution quality estimate total_estimate0.8656
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.7
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.310
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha153700000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.720

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)