Research workbench
AlphaFold monomer V2.0 prediction for NADPH-dependent D-xylose reductase II,III (P87039)
Analyse AlphaFold monomer V2.0 prediction for NADPH-dependent D-xylose reductase II,III… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P87039
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7A816d16baC3b20dEBc7EBDBDf668ce411f65C73
- Molecule
- NADPH-dependent D-xylose reductase II,III
- UniProt
- P87039
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent D-xylose reductase II,III | protein | 324 | 40% helix, 15% strand | P87039 |
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 | 363 | 0.69 | 0.82 | 46 | empty |
| 2 | 71 | 0.31 | 0.74 | 18 | 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 P87039
- Elsewhere: UniProt P87039 · AlphaFold DB P87039
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