Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase yvbk (O32248)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase yvbk… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O32248
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8a979B6826895aA149e9438c980E13ef9Ba70A5D
- Molecule
- Uncharacterized N-acetyltransferase yvbk
- UniProt
- O32248
- Pockets
- 1 · best druggability 0.68
Structure
1 distinct chain · 32% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized N-acetyltransferase yvbk | protein | 155 | 32% helix, 37% strand | O32248 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 492 | 0.68 | 0.79 | 51 | empty |
Compared structures
- 1YVK · Crystal Structure of the Bacillis subtilis Acetyltransferase in complex with CoA… · an experimental structure of the same protein · chain A against A, TM-score 0.95
- 1YVK · Crystal structure of the bacillis subtilis acetyltransferase in complex with CoA… · an experimental structure of the same protein · chain A against A, TM-score 0.95
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 O32248
- Elsewhere: UniProt O32248 · AlphaFold DB O32248
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