MolNFT v1 · #502032 · protein
AlphaFold monomer V2.0 prediction for NADPH-dependent D-xylose reductase (Q8X195)
Q8X195: “AlphaFold monomer V2.0 prediction for NADPH-dependent D-xylose reductase (Q8X195)”. 2 pockets (best druggability 0.68). MolNFT v1 #502032 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q8X195
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- NADPH-dependent D-xylose reductase
- UniProt
- Q8X195
- Pockets
- 2 · best druggability 0.68
Structure
1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent D-xylose reductase | protein | 321 | 41% helix, 16% strand | Q8X195 |
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 | 343 | 0.68 | 0.82 | 45 | empty |
| 2 | 63 | 0.29 | 0.74 | 15 | 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 Q8X195
- Elsewhere: UniProt Q8X195 · AlphaFold DB Q8X195
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