Research workbench
AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (Q3BCR3)
Analyse AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (Q3BCR3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q3BCR3
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd34DD3DBbC95510c872aD7e41A651f650Bd07472
- Molecule
- Thiopurine S-methyltransferase
- UniProt
- Q3BCR3
- Pockets
- 1 · best druggability 0.76
Structure
1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiopurine S-methyltransferase | protein | 245 | 30% helix, 26% strand | Q3BCR3 |
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 | 362 | 0.76 | 0.86 | 55 | 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 Q3BCR3
- Elsewhere: UniProt Q3BCR3 · AlphaFold DB Q3BCR3
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