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Crystal structure of human SULT1A1 bound to pap and two 3-cyano-7- hydroxycoumarin

Analyse Crystal structure of human SULT1A1 bound to pap and two 3-cyano-7… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3U3O
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sulfotransferase 1A1
EC: 2.8.2.1
UniProt: P50225
Ligands: 3QV, A3P
Pockets: 1 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sulfotransferase 1A1 (EC 2.8.2.1)	protein	288	44% helix, 11% strand	P50225

Ligands and binding sites

3QV · 7-hydroxy-2-oxo-2H-chromene-3-carbonitrile · ligand · 2 copies · chains A
A3P · Adenosine-3'-5'-diphosphate · 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	389	0.84	0.92	62	3QV, A3P

Compared structures

3U3O · Crystal structure of Human SULT1A1 bound to PAP and two 3-Cyano-7-hydroxycoumarin · the same entry in another collection · chain A against A, TM-score 1.00
P50225 · AlphaFold monomer V2.0 prediction for sulfotransferase 1A1 (P50225) · a predicted model of the same protein · 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 P50225
Elsewhere: RCSB PDB 3U3O · PDBe 3U3O · UniProt P50225

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