Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase I,II (O13283)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase I,II… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O13283
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA458d67e82B7FfA0Ce634c4b82799b47bE04B1a0
- Molecule
- NAD(P)H-dependent D-xylose reductase I,II
- UniProt
- O13283
- Pockets
- 1 · best druggability 0.69
Structure
1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-dependent D-xylose reductase I,II | protein | 324 | 40% helix, 15% strand | O13283 |
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 | 351 | 0.69 | 0.82 | 44 | 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 O13283
- Elsewhere: UniProt O13283 · AlphaFold DB O13283
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