Research workbench
AlphaFold monomer V2.0 prediction for glycerol-3-phosphate acyltransferase (A5F9D1)
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
- A5F9D1
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4925F35C539c838F29Bff8dbDd7f50009BD3f044
- Molecule
- Glycerol-3-phosphate acyltransferase
- UniProt
- A5F9D1
- Pockets
- 1 · best druggability 0.76
Structure
1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate acyltransferase | protein | 208 | 74% helix, 0% strand | A5F9D1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 341 | 0.76 | 0.87 | 53 | 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 A5F9D1
- Elsewhere: UniProt A5F9D1 · AlphaFold DB A5F9D1
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