Research workbench

Crystal structure of the human vitamin D receptor (H305F/H397F) ligand binding domain complexed with tei-9647

Analyse Crystal structure of the human vitamin D receptor (H305F/H397F) ligand binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3A2J
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: TEJ
Pockets: 1 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vitamin D3 receptor	protein	253	63% helix, 3% strand	P11473

Ligands and binding sites

TEJ · (1S,3R,5Z,7E,20S,23S)-1,3-dihydroxy-23,26-epoxy-9,10-secocholesta-5,7,10,25(27)-tetraen-26-one · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	288	0.86	0.96	36	TEJ

Compared structures

3A2J · Crystal structure of the human vitamin D receptor (H305F/H397F) ligand binding domain… · the same entry in another collection · chain A against A, TM-score 1.00
P11473 · AlphaFold monomer V2.0 prediction for vitamin D3 receptor (P11473) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 3A2J · PDBe 3A2J · UniProt P11473

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.