Research workbench
AlphaFold monomer V2.0 prediction for probable NAD(P)H-dependent D-xylose reductase XYL1 (Q4WJT9)
Analyse AlphaFold monomer V2.0 prediction for probable NAD(P)H-dependent D-xylose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4WJT9
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8F9c7747101075C570E34CAd4Ed2A4C01e9b2C28
- Molecule
- Probable NAD(P)H-dependent D-xylose reductase XYL1
- UniProt
- Q4WJT9
- Pockets
- 2 · best druggability 0.71
Structure
1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable NAD(P)H-dependent D-xylose reductase XYL1 | protein | 315 | 43% helix, 15% strand | Q4WJT9 |
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 | 398 | 0.71 | 0.82 | 46 | empty |
| 2 | 51 | 0.28 | 0.75 | 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 Q4WJT9
- Elsewhere: UniProt Q4WJT9 · AlphaFold DB Q4WJT9
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