Research workbench
AlphaFold monomer V2.0 prediction for 1-acyl-sn-glycerol-3-phosphate acyltransferase (Q42670)
Analyse AlphaFold monomer V2.0 prediction for 1-acyl-sn-glycerol-3-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q42670
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- UniProt
- Q42670
- Pockets
- 2 · best druggability 0.73
Structure
1 distinct chain · 43% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1-acyl-sn-glycerol-3-phosphate acyltransferase | protein | 308 | 43% helix, 12% strand | Q42670 |
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 | 563 | 0.73 | 0.81 | 54 | empty |
| 2 | 77 | 0.47 | 0.82 | 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 Q42670
- Elsewhere: UniProt Q42670 · AlphaFold DB Q42670
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