8xlk

Structure of native tri-heteromeric GluN1-GluN2A-GluN2B NMDA receptor in rat cortex and hippocampus

Method: ELECTRON MICROSCOPY Dmax: 209.2 Å Quality: GOOD

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

Glutamate receptor ionotropic, NMDA 1

OrganismNot specified

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 Other combination Heteromer Protein × 12 其他Polymer 3 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–938 Chain C; UniProt 1–938 Not recorded Glutamate receptor ionotropic, NMDA 2A × 1 (Q00959) Glutamate receptor ionotropic, NMDA 2B × 1 (Q00960) Heavy Chain of GluN1 Fab, 4F11 × 2 Light Chain of GluN1 Fab, 4F11 × 2 Heavy Chain of GluN2A Fab, 28C × 1 Light Chain of GluN2A Fab, 28C × 1 Heavy Chain of GluN2B Fab2 × 1 Light Chain of GluN2B Fab2 × 1 alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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 × 20 7RC (2R)-4-(3-phosphonopropyl)piperazine-2-carboxylic acid × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 1–938; UniProt 1–938 Author chain C; PDBConstruct 1–938; UniProt 1–938

Glutamate receptor ionotropic, NMDA 2A

OrganismNot specified

UniProt Q00959

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 × 12 其他Polymer 3 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–1464 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (P35439) Glutamate receptor ionotropic, NMDA 2B × 1 (Q00960) Heavy Chain of GluN1 Fab, 4F11 × 2 Light Chain of GluN1 Fab, 4F11 × 2 Heavy Chain of GluN2A Fab, 28C × 1 Light Chain of GluN2A Fab, 28C × 1 Heavy Chain of GluN2B Fab2 × 1 Light Chain of GluN2B Fab2 × 1 alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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 × 20 7RC (2R)-4-(3-phosphonopropyl)piperazine-2-carboxylic acid × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1464; UniProt 1–1464

Glutamate receptor ionotropic, NMDA 2B

OrganismNot specified

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 Other combination Heteromer Protein × 12 其他Polymer 3 PDB declaration: dodecameric(12) Consistent with protein copy count Chain D; UniProt 1–1482 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (P35439) Glutamate receptor ionotropic, NMDA 2A × 1 (Q00959) Heavy Chain of GluN1 Fab, 4F11 × 2 Light Chain of GluN1 Fab, 4F11 × 2 Heavy Chain of GluN2A Fab, 28C × 1 Light Chain of GluN2A Fab, 28C × 1 Heavy Chain of GluN2B Fab2 × 1 Light Chain of GluN2B Fab2 × 1 alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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 × 20 7RC (2R)-4-(3-phosphonopropyl)piperazine-2-carboxylic acid × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 3
Chains and sequence ranges 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 8xlk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8xlk
Deposition date deposition_date2023-12-26
Structure title titleStructure of native tri-heteromeric GluN1-GluN2A-GluN2B NMDA receptor in rat cortex and hippocampus
Keywords keywordsMEMBRANE PROTEIN, native NMDA receptor, adult rat cartex & hippocampus, GluN2A, GluN2B, MEMBRANE PROTEIN-IMMUNE SYSTEM complex; MEMBRANE PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.58
Radius of gyration Rg (electron density) rg_electron61.81
Forward intensity I(0) i03253710000.00
Molecular weight molecular_weight484820.0 kDa
Excluded volume excluded_volume608470 ų
Envelope volume envelope_volume928650 ų
Hydration-shell volume shell_volume127550 ų
Envelope diameter envelope_diameter204.2
Shell Rg shell_rg61.30
Envelope Rg envelope_rg61.10
Shape Rg shape_rg61.83
Total Rg total_rg61.73
Total atoms total_atoms34118
Residues n_residues4301
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 dmax209.2
Rg (real space) rg_real61.42
Rg uncertainty (real space) rg_real_error2.56
I(0) (real space) i0_real3.2540e+09
I(0) uncertainty (real space) i0_real_error6.7210e+07
Rg (reciprocal space) rg_reciprocal61.68
I(0) (reciprocal space) i0_reciprocal3255000000.0000
Solution quality estimate total_estimate0.8820
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.3
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.546
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha178400000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.881

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)