Research workbench
AlphaFold monomer V2.0 prediction for NADPH-dependent D-xylose reductase (O94735)
Analyse AlphaFold monomer V2.0 prediction for NADPH-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
- O94735
- Type
- protein
- Length
- 317 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB5268aA94a7047738311f34fD805c7fe3F299d8D
- Molecule
- NADPH-dependent D-xylose reductase
- UniProt
- O94735
- Pockets
- 2 · best druggability 0.67
Structure
1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent D-xylose reductase | protein | 317 | 44% helix, 15% strand | O94735 |
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 | 352 | 0.67 | 0.81 | 48 | empty |
| 2 | 83 | 0.32 | 0.74 | 17 | 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 O94735
- Elsewhere: UniProt O94735 · AlphaFold DB O94735
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