Research workbench
AlphaFold monomer V2.0 prediction for putative D-xylulose reductase (Q98D10)
Analyse AlphaFold monomer V2.0 prediction for putative D-xylulose reductase (Q98D10) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q98D10
- Type
- protein
- Length
- 348 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- Putative D-xylulose reductase
- UniProt
- Q98D10
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative D-xylulose reductase | protein | 348 | 30% helix, 29% strand | Q98D10 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 670 | 0.72 | 0.79 | 56 | empty |
| 2 | 98 | 0.45 | 0.79 | 20 | empty |
| 3 | 81 | 0.40 | 0.78 | 18 | 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 Q98D10
- Elsewhere: UniProt Q98D10 · AlphaFold DB Q98D10
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