Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase YCF52 (P51192)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase YCF52… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P51192
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDfA35f0a55525d00318dd861772da3C33F137075
- Molecule
- Uncharacterized N-acetyltransferase YCF52
- UniProt
- P51192
- Pockets
- 3 · best druggability 0.55
Structure
1 distinct chain · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized N-acetyltransferase YCF52 | protein | 174 | 31% helix, 27% strand | P51192 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.55 | 0.76 | 28 | empty |
| 2 | 177 | 0.52 | 0.78 | 24 | empty |
| 3 | 213 | 0.51 | 0.76 | 29 | 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 P51192
- Elsewhere: UniProt P51192 · AlphaFold DB P51192
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