Research workbench
AlphaFold monomer V2.0 prediction for hydroxylamine reductase (Q9X0Q4)
Analyse AlphaFold monomer V2.0 prediction for hydroxylamine reductase (Q9X0Q4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9X0Q4
- Type
- protein
- Length
- 431 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC454Ee1D7BbEeEfB51BeDA473EEF401822a07027
- Molecule
- Hydroxylamine reductase
- UniProt
- Q9X0Q4
- Pockets
- 6 · best druggability 0.74
Structure
1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxylamine reductase | protein | 431 | 47% helix, 16% strand | Q9X0Q4 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.74 | 0.93 | 37 | empty |
| 2 | 68 | 0.43 | 0.81 | 18 | empty |
| 3 | 96 | 0.40 | 0.77 | 19 | empty |
| 4 | 85 | 0.38 | 0.77 | 20 | empty |
| 5 | 60 | 0.33 | 0.76 | 13 | 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 Q9X0Q4
- Elsewhere: UniProt Q9X0Q4 · AlphaFold DB Q9X0Q4
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