Research workbench
AlphaFold monomer V2.0 prediction for formate acetyltransferase (Q59934)
Analyse AlphaFold monomer V2.0 prediction for formate acetyltransferase (Q59934) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q59934
- Type
- protein
- Length
- 775 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Formate acetyltransferase
- UniProt
- Q59934
- Pockets
- 10 · best druggability 0.70
Structure
1 distinct chain · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formate acetyltransferase | protein | 775 | 47% helix, 12% strand | Q59934 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.70 | 0.82 | 50 | empty |
| 2 | 50 | 0.69 | 0.97 | 17 | empty |
| 3 | 109 | 0.63 | 0.88 | 34 | empty |
| 4 | 216 | 0.61 | 0.81 | 35 | empty |
| 5 | 137 | 0.59 | 0.84 | 23 | 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 Q59934
- Elsewhere: UniProt Q59934 · AlphaFold DB Q59934
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