Research workbench
AlphaFold monomer V2.0 prediction for ion-translocating oxidoreductase complex subunit D (Q9HYB7)
Analyse AlphaFold monomer V2.0 prediction for ion-translocating oxidoreductase complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9HYB7
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf506A7D0abAEeA4fB2c7941B1a712c251c7EF300
- Molecule
- Ion-translocating oxidoreductase complex subunit D
- UniProt
- Q9HYB7
- Pockets
- 3 · best druggability 0.80
Structure
1 distinct chain · 61% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ion-translocating oxidoreductase complex subunit D | protein | 344 | 61% helix, 2% strand | Q9HYB7 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 281 | 0.80 | 0.91 | 40 | empty |
| 2 | 200 | 0.71 | 0.88 | 34 | empty |
| 3 | 84 | 0.37 | 0.76 | 17 | 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 Q9HYB7
- Elsewhere: UniProt Q9HYB7 · AlphaFold DB Q9HYB7
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