Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase (P78736)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P78736
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- NAD(P)H-dependent D-xylose reductase
- UniProt
- P78736
- Pockets
- 1 · best druggability 0.71
Structure
1 distinct chain · 41% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-dependent D-xylose reductase | protein | 318 | 41% helix, 14% strand | P78736 |
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 | 314 | 0.71 | 0.84 | 47 | 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 P78736
- Elsewhere: UniProt P78736 · AlphaFold DB P78736
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