Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized methyltransferase AN0656 (Q5BFM4)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized methyltransferase AN0656… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5BFM4
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1FdF165eB42e29a6686Ef2Ac96F71Aab73034EDE
- Molecule
- Uncharacterized methyltransferase AN0656
- UniProt
- Q5BFM4
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized methyltransferase AN0656 | protein | 286 | 39% helix, 20% strand | Q5BFM4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.76 | 0.95 | 28 | empty |
| 2 | 109 | 0.59 | 0.86 | 26 | empty |
| 3 | 55 | 0.35 | 0.78 | 20 | 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 Q5BFM4
- Elsewhere: UniProt Q5BFM4 · AlphaFold DB Q5BFM4
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