Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (Q1QD95)
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
- Q1QD95
- Type
- protein
- Length
- 591 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xFe0F6F52e06108B713093Cf01406F947Bc410fED
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- Q1QD95
- Pockets
- 8 · best druggability 0.65
Structure
1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C/D | protein | 591 | 42% helix, 16% strand | Q1QD95 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 305 | 0.65 | 0.80 | 44 | empty |
| 2 | 208 | 0.50 | 0.76 | 27 | empty |
| 3 | 140 | 0.47 | 0.77 | 16 | empty |
| 4 | 50 | 0.41 | 0.82 | 14 | empty |
| 5 | 86 | 0.38 | 0.76 | 20 | 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 Q1QD95
- Elsewhere: UniProt Q1QD95 · AlphaFold DB Q1QD95
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