Research workbench
AlphaFold monomer V2.0 prediction for phosphate acyltransferase (B2S523)
Analyse AlphaFold monomer V2.0 prediction for phosphate acyltransferase (B2S523) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2S523
- Type
- protein
- Length
- 346 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6fb11c21B6498d13235E1E54CC6363D32c6C7112
- Molecule
- Phosphate acyltransferase
- UniProt
- B2S523
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 51% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphate acyltransferase | protein | 346 | 51% helix, 17% strand | B2S523 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 498 | 0.66 | 0.77 | 51 | empty |
| 2 | 58 | 0.37 | 0.79 | 15 | empty |
| 3 | 52 | 0.27 | 0.74 | 11 | 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 B2S523
- Elsewhere: UniProt B2S523 · AlphaFold DB B2S523
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