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AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (P51580)

Analyse AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (P51580) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P51580
Type: protein
Length: 245 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x04362FE85E29D99f21630583f4F3B6E962DCb76C
Molecule: Thiopurine S-methyltransferase
UniProt: P51580
Pockets: 1 · best druggability 0.78

Structure

1 distinct chain · 29% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thiopurine S-methyltransferase	protein	245	29% helix, 26% strand	P51580

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	336	0.78	0.88	54	empty

Compared structures

2BZG · Crystal structure of thiopurine S-methyltransferase. · an experimental structure of the same protein · chain A against A, TM-score 0.93
2BZG · Crystal structure of thiopurine S-methyltransferase. · an experimental structure of the same protein · chain A against A, TM-score 0.93

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 P51580
Elsewhere: UniProt P51580 · AlphaFold DB P51580

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