Research workbench
AlphaFold monomer V2.0 prediction for TAGATURONATE/FRUCTURONATE epimerase (Q9WYS1)
Analyse AlphaFold monomer V2.0 prediction for TAGATURONATE/FRUCTURONATE epimerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9WYS1
- Type
- protein
- Length
- 481 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa39B2015befF3243019A855540D161D74D3E92C6
- Molecule
- TAGATURONATE/FRUCTURONATE epimerase
- UniProt
- Q9WYS1
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 51% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TAGATURONATE/FRUCTURONATE epimerase | protein | 481 | 51% helix, 17% strand | Q9WYS1 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 235 | 0.69 | 0.86 | 35 | empty |
| 2 | 139 | 0.51 | 0.80 | 28 | empty |
| 3 | 71 | 0.28 | 0.73 | 16 | 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 Q9WYS1
- Elsewhere: UniProt Q9WYS1 · AlphaFold DB Q9WYS1
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