Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase SCO2625 (Q9F309)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9F309
- Type
- protein
- Length
- 413 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x44aFAEAfE0F18812221E4762a1fA969072479765
- Molecule
- Uncharacterized N-acetyltransferase SCO2625
- UniProt
- Q9F309
- Pockets
- 2 · best druggability 0.70
Structure
1 distinct chain · 32% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized N-acetyltransferase SCO2625 | protein | 413 | 32% helix, 34% strand | Q9F309 |
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 | 762 | 0.70 | 0.77 | 72 | empty |
| 2 | 129 | 0.51 | 0.80 | 25 | 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 Q9F309
- Elsewhere: UniProt Q9F309 · AlphaFold DB Q9F309
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