8y1v

Structure of GluN1b-GluN2D NMDA receptor in complex with competitive antagonist R-CPP and allosteric inhibitor YY-23

Method: ELECTRON MICROSCOPY Dmax: 179.6 Å Quality: GOOD

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

Isoform 6 of 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 1–868 Chain C; UniProt 1–868 Not recorded Glutamate receptor ionotropic, NMDA 2D × 2 (O15399) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 A1LW8 (2~{R},3~{S},4~{S},5~{R},6~{R})-2-(hydroxymethyl)-6-[(2~{S})-2-methyl-4-[(1~{R},2~{R},4~{S},6~{S},7~{S},8~{R},9~{S},12~{S},13~{R},16~{S},18~{R})-7,9,13,18-tetramethyl-16-oxidanyl-5-oxapentacyclo[10.8.0.0^{2,9}.0^{4,8}.0^{13,18}]icosan-6-yl]butoxy]oxane-3,4,5-triol × 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.

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 Q05586-6
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–868; UniProt 1–868 Author chain C; PDBConstruct 1–868; UniProt 1–868

Glutamate receptor ionotropic, NMDA 2D

Homo sapiens

UniProt O15399

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 1–879 Chain D; UniProt 1–879 Not recorded Isoform 6 of Glutamate receptor ionotropic, NMDA 1 × 2 (Q05586) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 A1LW8 (2~{R},3~{S},4~{S},5~{R},6~{R})-2-(hydroxymethyl)-6-[(2~{S})-2-methyl-4-[(1~{R},2~{R},4~{S},6~{S},7~{S},8~{R},9~{S},12~{S},13~{R},16~{S},18~{R})-7,9,13,18-tetramethyl-16-oxidanyl-5-oxapentacyclo[10.8.0.0^{2,9}.0^{4,8}.0^{13,18}]icosan-6-yl]butoxy]oxane-3,4,5-triol × 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–879; UniProt 1–879 Author chain D; PDBConstruct 1–879; UniProt 1–879

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 8y1v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8y1v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8y1v
Deposition date deposition_date2024-01-25
Structure title titleStructure of GluN1b-GluN2D NMDA receptor in complex with competitive antagonist R-CPP and allosteric inhibitor YY-23
Keywords keywordsion channel, calcium permeable, glutamate receptor, neuronal expression, MEMBRANE PROTEIN, MEMBRANE PROTEIN-INHIBITOR complex; MEMBRANE PROTEIN/INHIBITOR
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.06
Radius of gyration Rg (electron density) rg_electron54.86
Forward intensity I(0) i01121320000.00
Molecular weight molecular_weight249520.0 kDa
Excluded volume excluded_volume297780 ų
Envelope volume envelope_volume587880 ų
Hydration-shell volume shell_volume94262 ų
Envelope diameter envelope_diameter182.6
Shell Rg shell_rg53.89
Envelope Rg envelope_rg52.52
Shape Rg shape_rg55.21
Total Rg total_rg53.78
Total atoms total_atoms31979
Residues n_residues2760
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 dmax179.6
Rg (real space) rg_real54.06
Rg uncertainty (real space) rg_real_error1.63
I(0) (real space) i0_real1.1210e+09
I(0) uncertainty (real space) i0_real_error2.2180e+07
Rg (reciprocal space) rg_reciprocal54.05
I(0) (reciprocal space) i0_reciprocal1121000000.0000
Solution quality estimate total_estimate0.8548
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.1
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.269
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha93320000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.492

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)