Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C (Q9PGJ3)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9PGJ3
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8FeAE72981819e83670F6a0fa7583C3e32901c2D
- Molecule
- NADH-quinone oxidoreductase subunit C
- UniProt
- Q9PGJ3
- Pockets
- 3 · best druggability 0.41
Structure
1 distinct chain · 19% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C | protein | 250 | 19% helix, 27% strand | Q9PGJ3 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.41 | 0.75 | 25 | empty |
| 2 | 60 | 0.30 | 0.75 | 14 | empty |
| 3 | 52 | 0.25 | 0.73 | 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 Q9PGJ3
- Elsewhere: UniProt Q9PGJ3 · AlphaFold DB Q9PGJ3
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