Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (Q88FH5)
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
- Q88FH5
- Type
- protein
- Length
- 593 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdd2B5c5c9c628759C36F2a51Baa6a4669F366E6d
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- Q88FH5
- Pockets
- 4 · best druggability 0.59
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 | Q88FH5 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 332 | 0.59 | 0.77 | 42 | empty |
| 2 | 163 | 0.48 | 0.77 | 26 | empty |
| 3 | 127 | 0.46 | 0.78 | 20 | empty |
| 4 | 65 | 0.28 | 0.73 | 12 | 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 Q88FH5
- Elsewhere: UniProt Q88FH5 · AlphaFold DB Q88FH5
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