Research workbench
AlphaFold monomer V2.0 prediction for probable D-xylulose reductase a (A1D9C9)
Analyse AlphaFold monomer V2.0 prediction for probable D-xylulose reductase a (A1D9C9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1D9C9
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0E5d19AAbEf43d610964131Fe6042A63EE0dd81A
- Molecule
- Probable D-xylulose reductase a
- UniProt
- A1D9C9
- Pockets
- 4 · best druggability 0.72
Structure
1 distinct chain · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable D-xylulose reductase a | protein | 358 | 31% helix, 28% strand | A1D9C9 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 554 | 0.72 | 0.80 | 48 | empty |
| 2 | 185 | 0.47 | 0.75 | 24 | empty |
| 3 | 112 | 0.38 | 0.74 | 17 | empty |
| 4 | 74 | 0.37 | 0.77 | 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 A1D9C9
- Elsewhere: UniProt A1D9C9 · AlphaFold DB A1D9C9
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