Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase SAV_4024 (Q82G74)
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
- Q82G74
- Type
- protein
- Length
- 418 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa5c421143c0C3c8674B862e86A6772B81f7Aef95
- Molecule
- Uncharacterized N-acetyltransferase SAV_4024
- UniProt
- Q82G74
- Pockets
- 3 · best druggability 0.73
Structure
1 distinct chain · 32% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized N-acetyltransferase SAV_4024 | protein | 418 | 32% helix, 32% strand | Q82G74 |
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 | 805 | 0.73 | 0.78 | 73 | empty |
| 2 | 188 | 0.50 | 0.77 | 25 | empty |
| 3 | 98 | 0.36 | 0.75 | 22 | 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 Q82G74
- Elsewhere: UniProt Q82G74 · AlphaFold DB Q82G74
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