Research workbench
AlphaFold monomer V2.0 prediction for validoxylamine a glucosyltransferase (Q15JF5)
Analyse AlphaFold monomer V2.0 prediction for validoxylamine a glucosyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q15JF5
- Type
- protein
- Length
- 453 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x619F51Fb686eB178E60C23E8610260c3C69601D6
- Molecule
- Validoxylamine a glucosyltransferase
- UniProt
- Q15JF5
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Validoxylamine a glucosyltransferase | protein | 453 | 35% helix, 17% strand | Q15JF5 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 251 | 0.76 | 0.89 | 39 | empty |
| 2 | 513 | 0.59 | 0.74 | 55 | empty |
| 3 | 53 | 0.43 | 0.83 | 14 | empty |
| 4 | 170 | 0.41 | 0.73 | 25 | empty |
| 5 | 58 | 0.31 | 0.76 | 15 | 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 Q15JF5
- Elsewhere: UniProt Q15JF5 · AlphaFold DB Q15JF5
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