Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase ylbp (O34468)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase ylbp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O34468
- Type
- protein
- Length
- 160 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- Uncharacterized N-acetyltransferase ylbp
- UniProt
- O34468
- Pockets
- 1 · best druggability 0.55
Structure
1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized N-acetyltransferase ylbp | protein | 160 | 30% helix, 27% strand | O34468 |
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 | 256 | 0.55 | 0.77 | 30 | empty |
Compared structures
- 2PR1 · Crystal structure of the Bacillus subtilis N-acetyltransferase YlbP protein in complex… · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 2PR1 · Crystal structure of the bacillus subtilis N-acetyltransferase ylbp protein in complex… · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 O34468
- Elsewhere: UniProt O34468 · AlphaFold DB O34468
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.