6whu

GluN1b-GluN2B NMDA receptor in complex with SDZ 220-040 and L689,560, class 1

Method: ELECTRON MICROSCOPY Dmax: 187.7 Å Quality: GOOD

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

Glutamate receptor ionotropic, NMDA 1

Rattus norvegicus

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 × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–959 Chain C; UniProt 1–959 Not recorded Glutamate receptor ionotropic, NMDA 2B × 2 (Q00960) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 QGM (2R,4S)-5,7-dichloro-4-[(phenylcarbamoyl)amino]-1,2,3,4-tetrahydroquinoline-2-carboxylic acid × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 QGP (2S)-2-amino-3-[2',4'-dichloro-4-hydroxy-5-(phosphonomethyl)biphenyl-3-yl]propanoic acid × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 P35439-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–959; UniProt 1–959 Author chain C; PDBConstruct 1–959; UniProt 1–959

Glutamate receptor ionotropic, NMDA 2B

Rattus norvegicus

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 × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 27–852 Chain D; UniProt 27–852 Not recorded Glutamate receptor ionotropic, NMDA 1 × 2 (P35439) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 QGM (2R,4S)-5,7-dichloro-4-[(phenylcarbamoyl)amino]-1,2,3,4-tetrahydroquinoline-2-carboxylic acid × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 QGP (2S)-2-amino-3-[2',4'-dichloro-4-hydroxy-5-(phosphonomethyl)biphenyl-3-yl]propanoic acid × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 2
Chains and sequence ranges Author chain B; PDBConstruct 58–883; UniProt 27–852 Author chain D; PDBConstruct 58–883; 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 6whu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6whu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6whu
Deposition date deposition_date2020-04-08
Structure title titleGluN1b-GluN2B NMDA receptor in complex with SDZ 220-040 and L689,560, class 1
Keywords keywords;NMDARs, Ligand-gated ion channels, METAL TRANSPORT, Ionotropic glutamate receptor, MEMBRANE PROTEIN, GluN1 antagonist, GluN2B antagonist ;; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.75
Radius of gyration Rg (electron density) rg_electron55.25
Forward intensity I(0) i01534300000.00
Molecular weight molecular_weight331840.0 kDa
Excluded volume excluded_volume416750 ų
Envelope volume envelope_volume654820 ų
Hydration-shell volume shell_volume102040 ų
Envelope diameter envelope_diameter187.7
Shell Rg shell_rg55.08
Envelope Rg envelope_rg54.19
Shape Rg shape_rg55.28
Total Rg total_rg55.13
Total atoms total_atoms23368
Residues n_residues3120
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 dmax187.7
Rg (real space) rg_real54.79
Rg uncertainty (real space) rg_real_error1.73
I(0) (real space) i0_real1.5340e+09
I(0) uncertainty (real space) i0_real_error2.9210e+07
Rg (reciprocal space) rg_reciprocal54.70
I(0) (reciprocal space) i0_reciprocal1534000000.0000
Solution quality estimate total_estimate0.8579
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.7
Skewness Skewness skewness0.377
Kurtosis Kurtosis kurtosis-0.246
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha194600000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.837; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.640

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)