Research workbench
AlphaFold monomer V2.0 prediction for palmitoyltransferase spe-10 (Q5FC64)
Analyse AlphaFold monomer V2.0 prediction for palmitoyltransferase spe-10 (Q5FC64) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5FC64
- Type
- protein
- Length
- 351 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x28e51F615E58598362D09182b4f56f5cAD52f49a
- Molecule
- Palmitoyltransferase spe-10
- UniProt
- Q5FC64
- Pockets
- 5 · best druggability 0.71
Structure
1 distinct chain · 56% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Palmitoyltransferase spe-10 | protein | 351 | 56% helix, 8% strand | Q5FC64 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.71 | 0.85 | 40 | empty |
| 2 | 411 | 0.60 | 0.76 | 34 | empty |
| 3 | 226 | 0.54 | 0.77 | 29 | empty |
| 4 | 143 | 0.46 | 0.77 | 20 | empty |
| 5 | 52 | 0.40 | 0.81 | 13 | 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 Q5FC64
- Elsewhere: UniProt Q5FC64 · AlphaFold DB Q5FC64
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