Research workbench
AlphaFold monomer V2.0 prediction for thialysine N-epsilon- acetyltransferase (Q7PCJ9)
Analyse AlphaFold monomer V2.0 prediction for thialysine N-epsilon- acetyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7PCJ9
- Type
- protein
- Length
- 170 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Thialysine N-epsilon-acetyltransferase
- UniProt
- Q7PCJ9
- Pockets
- 2 · best druggability 0.68
Structure
1 distinct chain · 40% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thialysine N-epsilon-acetyltransferase | protein | 170 | 40% helix, 24% strand | Q7PCJ9 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 481 | 0.68 | 0.79 | 43 | empty |
| 2 | 290 | 0.57 | 0.77 | 32 | 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 Q7PCJ9
- Elsewhere: UniProt Q7PCJ9 · AlphaFold DB Q7PCJ9
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