Research workbench
AlphaFold monomer V2.0 prediction for bifunctional udp-glucose 4-epimerase and udp-xylose 4-epimerase 1 (Q42605)
Analyse AlphaFold monomer V2.0 prediction for bifunctional udp-glucose 4-epimerase and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q42605
- Type
- protein
- Length
- 351 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd0F50FFcB725A32341066a3d047628d87754e5f8
- Molecule
- Bifunctional udp-glucose 4-epimerase and udp-xylose 4-epimerase 1
- UniProt
- Q42605
- Pockets
- 1 · best druggability 0.87
Structure
1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional udp-glucose 4-epimerase and udp-xylose 4-epimerase 1 | protein | 351 | 41% helix, 18% strand | Q42605 |
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 | 670 | 0.87 | 0.91 | 77 | 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 Q42605
- Elsewhere: UniProt Q42605 · AlphaFold DB Q42605
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