Research workbench
AlphaFold monomer V2.0 prediction for phosphate acetyltransferase (Q9RY77)
Analyse AlphaFold monomer V2.0 prediction for phosphate acetyltransferase (Q9RY77) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9RY77
- Type
- protein
- Length
- 702 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Phosphate acetyltransferase
- UniProt
- Q9RY77
- Pockets
- 8 · best druggability 0.68
Structure
1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphate acetyltransferase | protein | 702 | 45% helix, 17% strand | Q9RY77 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 376 | 0.68 | 0.81 | 40 | empty |
| 2 | 290 | 0.62 | 0.80 | 34 | empty |
| 3 | 232 | 0.56 | 0.78 | 27 | empty |
| 4 | 161 | 0.50 | 0.78 | 37 | empty |
| 5 | 109 | 0.46 | 0.79 | 17 | 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 Q9RY77
- Elsewhere: UniProt Q9RY77 · AlphaFold DB Q9RY77
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