MolNFT v1 · #502045 · protein
AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase (P31867)
P31867: “AlphaFold monomer V2.0 prediction for NAD(P)H-dependent D-xylose reductase (P31867)”. 1 pocket (best druggability 0.71). MolNFT v1 #502045 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P31867
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xeD1A6159e26791F22a6cE039130D208Ac313c418
- Molecule
- NAD(P)H-dependent D-xylose reductase
- UniProt
- P31867
- Pockets
- 1 · best druggability 0.71
Structure
1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-dependent D-xylose reductase | protein | 318 | 41% helix, 15% strand | P31867 |
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 | 339 | 0.71 | 0.83 | 43 | empty |
Compared structures
- 5Z6T · Crystal structure of D-xylose reductase from scheffersomyces stipitis in complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 5Z6U · Crystal structure of D-xylose reductase from scheffersomyces stipitis · an experimental structure of the same protein · chain A against A, TM-score 0.98
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 P31867
- Elsewhere: UniProt P31867 · AlphaFold DB P31867
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