Research workbench
AlphaFold monomer V2.0 prediction for lipid a palmitoyltransferase pagp (F2EP14)
Analyse AlphaFold monomer V2.0 prediction for lipid a palmitoyltransferase pagp (F2EP14) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F2EP14
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE83049713370f9cea2d2CDB16Db5b485De523e3A
- Molecule
- Lipid a palmitoyltransferase pagp
- UniProt
- F2EP14
- Pockets
- 1 · best druggability 0.65
Structure
1 distinct chain · 28% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipid a palmitoyltransferase pagp | protein | 190 | 28% helix, 47% strand | F2EP14 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.65 | 0.83 | 34 | 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 F2EP14
- Elsewhere: UniProt F2EP14 · AlphaFold DB F2EP14
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