Research workbench
AlphaFold monomer V2.0 prediction for fatty acid hydroxylase vlma (A0A024FA41)
Analyse AlphaFold monomer V2.0 prediction for fatty acid hydroxylase vlma (A0A024FA41) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A024FA41
- Type
- protein
- Length
- 365 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- Fatty acid hydroxylase vlma
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 55% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid hydroxylase vlma | protein | 365 | 55% helix, 2% strand | — |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.64 | 0.84 | 28 | empty |
| 2 | 104 | 0.40 | 0.76 | 19 | empty |
| 3 | 59 | 0.34 | 0.77 | 15 | empty |
| 4 | 51 | 0.32 | 0.77 | 12 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
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