Research workbench
AlphaFold monomer V2.0 prediction for glycerol-3-phosphate acyltransferase (A1UT26)
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
- A1UT26
- Type
- protein
- Length
- 211 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- Glycerol-3-phosphate acyltransferase
- UniProt
- A1UT26
- Pockets
- 2 · best druggability 0.68
Structure
1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate acyltransferase | protein | 211 | 73% helix, 0% strand | A1UT26 |
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 | 260 | 0.68 | 0.84 | 41 | empty |
| 2 | 52 | 0.35 | 0.78 | 12 | 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 A1UT26
- Elsewhere: UniProt A1UT26 · AlphaFold DB A1UT26
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