MolNFT v1 · #23348 · protein

Crystal structure of the vdr ligand binding domain complexed to TX522

1TXI · Vitamin D receptor: “Crystal structure of the vdr ligand binding domain complexed to TX522”. X-ray diffraction, 1 ligand (TX5), 2 pockets (best druggability 0.86). MolNFT v1 #23348 on GenesisL1: 3D structure, binding sites and…

PDB: 1TXI
Type: protein
Length: 253 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vitamin D receptor
UniProt: P11473
Ligands: TX5
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 D receptor	protein	253	66% helix, 3% strand	P11473

Ligands and binding sites

TX5 · (1R,3R)-5-((Z)-2-((1r,7as)-hexahydro-1-((S)-6-hydroxy-6-methylhept-4-yn-2-yl)-7A-methyl-1H-inden-4(7ah)-ylidene)ethylidene)cyclohexane-1,3-diol · 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	332	0.86	0.95	39	TX5
2	74	0.33	0.75	17	empty

Compared structures

1TXI · Crystal structure of the vdr ligand binding domain complexed to TX522 · 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 1TXI · PDBe 1TXI · UniProt P11473

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