5v39

Crystal structure of human vitamin D receptor ligand binding domain in complex with a VDRM

Method: X-RAY DIFFRACTION Dmax: 64.7 Å Quality: GOOD

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

Vitamin D3 receptor

Homo sapiens

UniProt P11473

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 169–475 Not recorded 8VM 5-(3-{4-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-3-methylphenyl}pentan-3-yl)-3-methyl-N-(1H-tetrazol-5-yl)thiophene-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;298 K;100mM Tris HCl pH 8.5, 25% PEG 3350 and 200mM Ammonium Sulfate Resolution 2.20 Å R-free 0.235

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.

51 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VDR_HUMAN
Isoform P11473-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–256; UniProt 169–475

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 5v39

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5v39
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5v39
Deposition date deposition_date2017-03-06
Structure title titleCrystal structure of human vitamin D receptor ligand binding domain in complex with a VDRM
Keywords keywordsVDR, LBD, VDRM, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.61
Radius of gyration Rg (electron density) rg_electron18.45
Forward intensity I(0) i014335100.00
Molecular weight molecular_weight28872.0 kDa
Excluded volume excluded_volume36383 ų
Envelope volume envelope_volume41491 ų
Hydration-shell volume shell_volume18891 ų
Envelope diameter envelope_diameter66.8
Shell Rg shell_rg24.63
Envelope Rg envelope_rg18.78
Shape Rg shape_rg18.43
Total Rg total_rg19.44
Total atoms total_atoms2025
Residues n_residues251
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 dmax64.7
Rg (real space) rg_real19.55
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real1.4340e+07
I(0) uncertainty (real space) i0_real_error1.8550e+05
Rg (reciprocal space) rg_reciprocal19.56
I(0) (reciprocal space) i0_reciprocal14340000.0000
Solution quality estimate total_estimate0.7979
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.299
Kurtosis Kurtosis kurtosis-0.228
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3116000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.791; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5v39a_
Class classa — All alpha proteins
Fold Fold folda.123 — Nuclear receptor ligand-binding domain
Superfamily Superfamily superfamilya.123.1 — Nuclear receptor ligand-binding domain
Family Family familya.123.1.1 — Nuclear receptor ligand-binding domain

CATH v4.4 (1 domains)

Domain ID domain_id5v39A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor

8. Citations (1)

9. Files and Curves (10)