Research workbench
AlphaFold monomer V2.0 prediction for palmitoyltransferase PFA5 (Q6FMP5)
Analyse AlphaFold monomer V2.0 prediction for palmitoyltransferase PFA5 (Q6FMP5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6FMP5
- Type
- protein
- Length
- 352 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x01174A58f4c65021971a156470Db815F4886F4b7
- Molecule
- Palmitoyltransferase PFA5
- UniProt
- Q6FMP5
- Pockets
- 5 · best druggability 0.71
Structure
1 distinct chain · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Palmitoyltransferase PFA5 | protein | 352 | 51% helix, 12% strand | Q6FMP5 |
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 | 289 | 0.71 | 0.84 | 31 | empty |
| 2 | 198 | 0.62 | 0.83 | 29 | empty |
| 3 | 118 | 0.55 | 0.83 | 25 | empty |
| 4 | 83 | 0.38 | 0.77 | 19 | empty |
| 5 | 61 | 0.29 | 0.75 | 16 | 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 Q6FMP5
- Elsewhere: UniProt Q6FMP5 · AlphaFold DB Q6FMP5
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