Research workbench
AlphaFold monomer V2.0 prediction for phosphate acyltransferase (Q87YG5)
Analyse AlphaFold monomer V2.0 prediction for phosphate acyltransferase (Q87YG5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q87YG5
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- Phosphate acyltransferase
- UniProt
- Q87YG5
- Pockets
- 4 · best druggability 0.60
Structure
1 distinct chain · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphate acyltransferase | protein | 340 | 50% helix, 18% strand | Q87YG5 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.60 | 0.81 | 35 | empty |
| 2 | 109 | 0.47 | 0.79 | 22 | empty |
| 3 | 122 | 0.42 | 0.76 | 19 | empty |
| 4 | 52 | 0.29 | 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 Q87YG5
- Elsewhere: UniProt Q87YG5 · AlphaFold DB Q87YG5
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