Research workbench
AlphaFold monomer V2.0 prediction for proton-translocating FERREDOXIN:NAD(+) oxidoreductase complex subunit C (D8GR66)
Analyse AlphaFold monomer V2.0 prediction for proton-translocating FERREDOXIN:NAD(+)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- D8GR66
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcBd878cACF8B1F59a9D92Dfb5b82Ad72Fd006916
- Molecule
- Proton-translocating FERREDOXIN:NAD(+) oxidoreductase complex subunit C
- UniProt
- D8GR66
- Pockets
- 3 · best druggability 0.79
Structure
1 distinct chain · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proton-translocating FERREDOXIN:NAD(+) oxidoreductase complex subunit C | protein | 457 | 32% helix, 21% strand | D8GR66 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 933 | 0.79 | 0.81 | 74 | empty |
| 2 | 397 | 0.66 | 0.79 | 32 | empty |
| 3 | 113 | 0.57 | 0.85 | 27 | 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 D8GR66
- Elsewhere: UniProt D8GR66 · AlphaFold DB D8GR66
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