Research workbench
AlphaFold monomer V2.0 prediction for probable NAD(P)H-dependent D-xylose reductase XYL1 (C5FFQ7)
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
- C5FFQ7
- Type
- protein
- Length
- 327 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0a5E8971Bc8668384f357c645750797DdfA6b629
- Molecule
- Probable NAD(P)H-dependent D-xylose reductase XYL1
- UniProt
- C5FFQ7
- Pockets
- 1 · best druggability 0.70
Structure
1 distinct chain · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable NAD(P)H-dependent D-xylose reductase XYL1 | protein | 327 | 40% helix, 14% strand | C5FFQ7 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 398 | 0.70 | 0.81 | 48 | 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 C5FFQ7
- Elsewhere: UniProt C5FFQ7 · AlphaFold DB C5FFQ7
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