Research workbench

Crystal structure of human dhea-st complexed with androsterone

Analyse Crystal structure of human dhea-st complexed with androsterone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OV4
Type: protein
Length: 267 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alcohol sulfotransferase
EC: 2.8.2.2
UniProt: Q06520
Ligands: AOX, SO4
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alcohol sulfotransferase (EC 2.8.2.2)	protein	267	49% helix, 11% strand	Q06520

Ligands and binding sites

AOX · (3Beta,5alpha)-3-Hydroxyandrostan-17-one · ligand · chains A
SO4 · Sulfate ion · ion · 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	693	0.72	0.78	73	SO4, AOX
2	159	0.44	0.75	25	empty

Compared structures

1OV4 · Crystal structure of human DHEA-ST complexed with androsterone · the same entry in another collection · chain A against A, TM-score 1.00
Q06520 · AlphaFold monomer V2.0 prediction for sulfotransferase 2A1 (Q06520) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q06520
Elsewhere: RCSB PDB 1OV4 · PDBe 1OV4 · UniProt Q06520

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