8e93

D-cycloserine and glutamate bound Human GluN1a-GluN2C NMDA receptor in splayed conformation

Method: ELECTRON MICROSCOPY Dmax: 174.7 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 Other combination Heteromer Protein × 4 其他Polymer 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–847 Chain C; UniProt 1–847 Not recorded Glutamate receptor ionotropic, NMDA 2C × 2 (Q14957) beta-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 × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.71 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 1–847; UniProt 1–847 Author chain C; PDBConstruct 1–847; UniProt 1–847

Glutamate receptor ionotropic, NMDA 2C

Homo sapiens

UniProt Q14957

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 × 4 其他Polymer 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 26–849 Chain D; UniProt 26–849 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (Q05586) beta-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 × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.71 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 57–880; UniProt 26–849 Author chain D; PDBConstruct 57–880; UniProt 26–849

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 8e93

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e93
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e93
Deposition date deposition_date2022-08-26
Structure title titleD-cycloserine and glutamate bound Human GluN1a-GluN2C NMDA receptor in splayed conformation
Keywords keywordsLigand-gated ion channel, ionotropic glutamate receptor, synaptic protein, voltage-gate ion channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.54
Radius of gyration Rg (electron density) rg_electron51.27
Forward intensity I(0) i0789948000.00
Molecular weight molecular_weight236140.0 kDa
Excluded volume excluded_volume296500 ų
Envelope volume envelope_volume481610 ų
Hydration-shell volume shell_volume79815 ų
Envelope diameter envelope_diameter184.7
Shell Rg shell_rg53.59
Envelope Rg envelope_rg49.80
Shape Rg shape_rg51.28
Total Rg total_rg51.34
Total atoms total_atoms16664
Residues n_residues2320
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 dmax174.7
Rg (real space) rg_real51.55
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real7.8990e+08
I(0) uncertainty (real space) i0_real_error1.7040e+07
Rg (reciprocal space) rg_reciprocal51.52
I(0) (reciprocal space) i0_reciprocal789900000.0000
Solution quality estimate total_estimate0.8774
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.0
Skewness Skewness skewness0.314
Kurtosis Kurtosis kurtosis-0.337
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77950000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.776

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)