Research workbench
AlphaFold monomer V2.0 prediction for D-xylulose reductase (Q59545)
Analyse AlphaFold monomer V2.0 prediction for D-xylulose reductase (Q59545) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q59545
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7746095A33F2b1CD4a2D513b839bb4B33c352C5C
- Molecule
- D-xylulose reductase
- UniProt
- Q59545
- Pockets
- 2 · best druggability 0.75
Structure
1 distinct chain · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-xylulose reductase | protein | 338 | 31% helix, 28% strand | Q59545 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1197 | 0.75 | 0.78 | 88 | empty |
| 2 | 67 | 0.35 | 0.78 | 17 | 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 Q59545
- Elsewhere: UniProt Q59545 · AlphaFold DB Q59545
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