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Structural basis for the accommodation of bis- and tris-aromatic derivatives in vitamin D nuclear receptor

Analyse Structural basis for the accommodation of bis- and tris-aromatic derivatives in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4G2I
Type: protein
Length: 253 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vitamin D3 receptor
UniProt: P11473
Ligands: 0VQ
Pockets: 2 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vitamin D3 receptor	protein	253	66% helix, 3% strand	P11473

Ligands and binding sites

0VQ · (3E,5E)-6-(3-{2-[3,4-bis(hydroxymethyl)phenyl]ethyl}phenyl)-1,1,1-trifluoro-2-(trifluoromethyl)octa-3,5-dien-2-ol · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	290	0.86	0.96	38	0VQ
2	71	0.33	0.75	18	empty

Compared structures

4G2I · Structural basis for the accommodation of bis- and tris-aromatic derivatives in Vitamin D… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P11473
Elsewhere: RCSB PDB 4G2I · PDBe 4G2I · UniProt P11473

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