Research workbench
AlphaFold monomer V2.0 prediction for formate acetyltransferase (Q46266)
Analyse AlphaFold monomer V2.0 prediction for formate acetyltransferase (Q46266) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q46266
- Type
- protein
- Length
- 740 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x16CCa6E3e9FB6F3BA58AD90F1CA9Ed23Cf6fc7d2
- Molecule
- Formate acetyltransferase
- UniProt
- Q46266
- Pockets
- 6 · best druggability 0.68
Structure
1 distinct chain · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formate acetyltransferase | protein | 740 | 48% helix, 13% strand | Q46266 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.68 | 0.92 | 24 | empty |
| 2 | 126 | 0.57 | 0.84 | 29 | empty |
| 3 | 218 | 0.57 | 0.79 | 35 | empty |
| 4 | 162 | 0.48 | 0.77 | 27 | empty |
| 5 | 61 | 0.41 | 0.81 | 14 | 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 Q46266
- Elsewhere: UniProt Q46266 · AlphaFold DB Q46266
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