Research workbench
AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (B0KUP7)
Analyse AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (B0KUP7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0KUP7
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Thiopurine S-methyltransferase
- UniProt
- B0KUP7
- Pockets
- 1 · best druggability 0.73
Structure
1 distinct chain · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiopurine S-methyltransferase | protein | 216 | 35% helix, 27% strand | B0KUP7 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.73 | 0.84 | 54 | empty |
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 B0KUP7
- Elsewhere: UniProt B0KUP7 · AlphaFold DB B0KUP7
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