Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase YCF52 (Q1XDU5)
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
- Q1XDU5
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Uncharacterized N-acetyltransferase YCF52
- UniProt
- Q1XDU5
- Pockets
- 3 · best druggability 0.57
Structure
1 distinct chain · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized N-acetyltransferase YCF52 | protein | 174 | 30% helix, 25% strand | Q1XDU5 |
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 | 343 | 0.57 | 0.75 | 28 | empty |
| 2 | 187 | 0.49 | 0.76 | 23 | empty |
| 3 | 140 | 0.45 | 0.76 | 18 | 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 Q1XDU5
- Elsewhere: UniProt Q1XDU5 · AlphaFold DB Q1XDU5
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