Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (A4WCR5)
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
- A4WCR5
- Type
- protein
- Length
- 595 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC71436dbe7D887e0980cA8E95ea8166A2915aE95
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- A4WCR5
- Pockets
- 7 · best druggability 0.58
Structure
1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C/D | protein | 595 | 44% helix, 17% strand | A4WCR5 |
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 | 224 | 0.58 | 0.80 | 26 | empty |
| 2 | 176 | 0.49 | 0.77 | 20 | empty |
| 3 | 157 | 0.48 | 0.77 | 24 | empty |
| 4 | 72 | 0.47 | 0.83 | 19 | empty |
| 5 | 184 | 0.44 | 0.74 | 26 | 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 A4WCR5
- Elsewhere: UniProt A4WCR5 · AlphaFold DB A4WCR5
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