Research workbench
AlphaFold monomer V2.0 prediction for platelet-activating factor acetylhydrolase 2, cytoplasmic (P79106)
Analyse AlphaFold monomer V2.0 prediction for platelet-activating factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P79106
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- UniProt
- P79106
- Pockets
- 3 · best druggability 0.64
Structure
1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Platelet-activating factor acetylhydrolase 2, cytoplasmic | protein | 392 | 35% helix, 21% strand | P79106 |
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 | 224 | 0.64 | 0.83 | 36 | empty |
| 2 | 135 | 0.46 | 0.77 | 25 | empty |
| 3 | 62 | 0.42 | 0.80 | 10 | 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 P79106
- Elsewhere: UniProt P79106 · AlphaFold DB P79106
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