Research workbench
AlphaFold monomer V2.0 prediction for probable NAD(P)H-dependent D-xylose reductase XYL1 (B8N195)
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
- B8N195
- Type
- protein
- Length
- 319 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- Probable NAD(P)H-dependent D-xylose reductase XYL1
- UniProt
- B8N195
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable NAD(P)H-dependent D-xylose reductase XYL1 | protein | 319 | 42% helix, 15% strand | B8N195 |
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 | 277 | 0.69 | 0.84 | 41 | empty |
| 2 | 53 | 0.31 | 0.76 | 20 | 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 B8N195
- Elsewhere: UniProt B8N195 · AlphaFold DB B8N195
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