Research workbench
AlphaFold monomer V2.0 prediction for phosphate acetyltransferase (P45107)
Analyse AlphaFold monomer V2.0 prediction for phosphate acetyltransferase (P45107) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P45107
- Type
- protein
- Length
- 711 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- Phosphate acetyltransferase
- UniProt
- P45107
- Pockets
- 6 · best druggability 0.77
Structure
1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphate acetyltransferase | protein | 711 | 44% helix, 18% strand | P45107 |
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 | 862 | 0.77 | 0.80 | 95 | empty |
| 2 | 429 | 0.67 | 0.79 | 40 | empty |
| 3 | 253 | 0.55 | 0.77 | 43 | empty |
| 4 | 160 | 0.44 | 0.75 | 29 | empty |
| 5 | 53 | 0.30 | 0.76 | 10 | 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 P45107
- Elsewhere: UniProt P45107 · AlphaFold DB P45107
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