Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase (Q9P430)
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
- Q9P430
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- NAD(P)H-dependent D-xylose reductase
- UniProt
- Q9P430
- Pockets
- 2 · best druggability 0.71
Structure
1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-dependent D-xylose reductase | protein | 323 | 39% helix, 15% strand | Q9P430 |
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 | 300 | 0.71 | 0.84 | 45 | empty |
| 2 | 80 | 0.32 | 0.74 | 19 | 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 Q9P430
- Elsewhere: UniProt Q9P430 · AlphaFold DB Q9P430
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