Research workbench
AlphaFold monomer V2.0 prediction for phosphate acyltransferase (A2S9Y1)
Analyse AlphaFold monomer V2.0 prediction for phosphate acyltransferase (A2S9Y1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2S9Y1
- Type
- protein
- Length
- 368 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Phosphate acyltransferase
- UniProt
- A2S9Y1
- Pockets
- 4 · best druggability 0.63
Structure
1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphate acyltransferase | protein | 368 | 44% helix, 16% strand | A2S9Y1 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.63 | 0.83 | 32 | empty |
| 2 | 215 | 0.62 | 0.82 | 33 | empty |
| 3 | 138 | 0.44 | 0.76 | 18 | empty |
| 4 | 52 | 0.24 | 0.72 | 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 A2S9Y1
- Elsewhere: UniProt A2S9Y1 · AlphaFold DB A2S9Y1
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