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AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (Q4ZRJ1)
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
- Q4ZRJ1
- Type
- protein
- Length
- 593 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x10F20E5FD6223F71224Fba7496Eba14cf3dd37D0
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- Q4ZRJ1
- Pockets
- 5 · best druggability 0.59
Structure
1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C/D | protein | 593 | 42% helix, 15% strand | Q4ZRJ1 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.59 | 0.80 | 28 | empty |
| 2 | 208 | 0.52 | 0.77 | 26 | empty |
| 3 | 158 | 0.48 | 0.77 | 18 | empty |
| 4 | 107 | 0.40 | 0.75 | 19 | empty |
| 5 | 69 | 0.31 | 0.74 | 13 | 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 Q4ZRJ1
- Elsewhere: UniProt Q4ZRJ1 · AlphaFold DB Q4ZRJ1
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