Research workbench
AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (Q5RBJ3)
Analyse AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (Q5RBJ3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RBJ3
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Thiopurine S-methyltransferase
- UniProt
- Q5RBJ3
- Pockets
- 1 · best druggability 0.78
Structure
1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiopurine S-methyltransferase | protein | 245 | 31% helix, 26% strand | Q5RBJ3 |
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 | 406 | 0.78 | 0.87 | 58 | 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 Q5RBJ3
- Elsewhere: UniProt Q5RBJ3 · AlphaFold DB Q5RBJ3
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