Research workbench
AlphaFold monomer V2.0 prediction for ion-translocating oxidoreductase complex subunit C (Q320Y6)
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
- Q320Y6
- Type
- protein
- Length
- 740 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Ion-translocating oxidoreductase complex subunit C
- UniProt
- Q320Y6
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ion-translocating oxidoreductase complex subunit C | protein | 740 | 47% helix, 12% strand | Q320Y6 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 929 | 0.75 | 0.78 | 67 | empty |
| 2 | 69 | 0.66 | 0.93 | 21 | empty |
| 3 | 432 | 0.60 | 0.76 | 36 | empty |
| 4 | 108 | 0.45 | 0.78 | 15 | 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 Q320Y6
- Elsewhere: UniProt Q320Y6 · AlphaFold DB Q320Y6
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