Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase XYL1 (Q876L8)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase XYL1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q876L8
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- NAD(P)H-dependent D-xylose reductase XYL1
- UniProt
- Q876L8
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-dependent D-xylose reductase XYL1 | protein | 324 | 42% helix, 15% strand | Q876L8 |
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 | 344 | 0.69 | 0.82 | 44 | empty |
| 2 | 57 | 0.27 | 0.74 | 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 Q876L8
- Elsewhere: UniProt Q876L8 · AlphaFold DB Q876L8
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