Research workbench
AlphaFold monomer V2.0 prediction for formate acetyltransferase (P43753)
Analyse AlphaFold monomer V2.0 prediction for formate acetyltransferase (P43753) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P43753
- Type
- protein
- Length
- 770 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4c95195895AF3DA8b373112E979f53d8821322f7
- Molecule
- Formate acetyltransferase
- UniProt
- P43753
- Pockets
- 5 · best druggability 0.74
Structure
1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formate acetyltransferase | protein | 770 | 46% helix, 14% strand | P43753 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.74 | 0.95 | 31 | empty |
| 2 | 198 | 0.55 | 0.79 | 24 | empty |
| 3 | 84 | 0.42 | 0.79 | 18 | empty |
| 4 | 95 | 0.37 | 0.75 | 16 | empty |
| 5 | 64 | 0.31 | 0.75 | 16 | 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 P43753
- Elsewhere: UniProt P43753 · AlphaFold DB P43753
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