Research workbench
AlphaFold monomer V2.0 prediction for alpha-(1,6)-fucosyltransferase (Q6EV77)
Analyse AlphaFold monomer V2.0 prediction for alpha-(1,6)-fucosyltransferase (Q6EV77) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6EV77
- Type
- protein
- Length
- 575 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc80b46AF78867fEDD81548116F7a1b91a9b8EA03
- Molecule
- Alpha-(1,6)-fucosyltransferase
- UniProt
- Q6EV77
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-(1,6)-fucosyltransferase | protein | 575 | 51% helix, 13% strand | Q6EV77 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.70 | 0.88 | 29 | empty |
| 2 | 616 | 0.67 | 0.76 | 59 | empty |
| 3 | 134 | 0.51 | 0.80 | 21 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q6EV77
- Elsewhere: UniProt Q6EV77 · AlphaFold DB Q6EV77
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