Research workbench
AlphaFold monomer V2.0 prediction for 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (Q9NRZ5)
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
- Q9NRZ5
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe4aF75CC6301a0Afa5dD04dd207fC9F42D188805
- Molecule
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- UniProt
- Q9NRZ5
- Pockets
- 3 · best druggability 0.86
Structure
1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1-acyl-sn-glycerol-3-phosphate acyltransferase delta | protein | 378 | 56% helix, 12% strand | Q9NRZ5 |
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 | 862 | 0.86 | 0.88 | 100 | empty |
| 2 | 95 | 0.36 | 0.74 | 21 | empty |
| 3 | 51 | 0.32 | 0.77 | 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 Q9NRZ5
- Elsewhere: UniProt Q9NRZ5 · AlphaFold DB Q9NRZ5
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