Research workbench
AlphaFold monomer V2.0 prediction for glycerol-3-phosphate acyltransferase (B1I461)
Analyse AlphaFold monomer V2.0 prediction for glycerol-3-phosphate acyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1I461
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd9E63dcE84b18c2c82d6102A25eE05c6718097CA
- Molecule
- Glycerol-3-phosphate acyltransferase
- UniProt
- B1I461
- Pockets
- 2 · best druggability 0.72
Structure
1 distinct chain · 75% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate acyltransferase | protein | 198 | 75% helix, 1% strand | B1I461 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 395 | 0.72 | 0.83 | 43 | empty |
| 2 | 58 | 0.28 | 0.74 | 15 | 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 B1I461
- Elsewhere: UniProt B1I461 · AlphaFold DB B1I461
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