Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (A4XV04)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4XV04
- Type
- protein
- Length
- 593 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaa881a9f97666A01Da48Ea02eAe65Ad17eb8B4F6
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- A4XV04
- Pockets
- 7 · best druggability 0.58
Structure
1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C/D | protein | 593 | 42% helix, 16% strand | A4XV04 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 227 | 0.58 | 0.79 | 27 | empty |
| 2 | 178 | 0.50 | 0.77 | 25 | empty |
| 3 | 140 | 0.49 | 0.78 | 19 | empty |
| 4 | 96 | 0.39 | 0.76 | 17 | empty |
| 5 | 73 | 0.34 | 0.76 | 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 A4XV04
- Elsewhere: UniProt A4XV04 · AlphaFold DB A4XV04
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