Research workbench
AlphaFold monomer V2.0 prediction for probable NAD(P)H-dependent D-xylose reductase XYL1 (A1CRI1)
Analyse AlphaFold monomer V2.0 prediction for probable NAD(P)H-dependent D-xylose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1CRI1
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x542cf37c74b0D14016ac38c89Ead959487C21d2B
- Molecule
- Probable NAD(P)H-dependent D-xylose reductase XYL1
- UniProt
- A1CRI1
- Pockets
- 5 · best druggability 0.74
Structure
1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable NAD(P)H-dependent D-xylose reductase XYL1 | protein | 330 | 44% helix, 15% strand | A1CRI1 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 294 | 0.74 | 0.87 | 46 | empty |
| 2 | 159 | 0.55 | 0.80 | 20 | empty |
| 3 | 63 | 0.31 | 0.75 | 19 | empty |
| 4 | 53 | 0.31 | 0.76 | 17 | empty |
| 5 | 51 | 0.26 | 0.73 | 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 A1CRI1
- Elsewhere: UniProt A1CRI1 · AlphaFold DB A1CRI1
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