UniProt A0A024L1E0
NADH-quinone oxidoreductase subunit C/D (A0A024L1E0)
NADH-quinone oxidoreductase subunit C/D (UniProt A0A024L1E0), EC 7.1.1.-: 7 experimental structures on GenesisL1, 3 ligands bound, 22 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A024L1E0
- Protein
- NADH-quinone oxidoreductase subunit C/D
- EC
- 7.1.1.-
- Experimental structures
- 7
- Predicted models
- 0
- Ligands
- 3
- Pockets
- 22 · 3 records with a druggable one
Structures
7 records of A0A024L1E0 in the MolNFT archive: 7 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 7AWT | E. coli NADH qui oxidoreductase hydrophilic arm | electron microscopy | D | SF4 | — |
| 7AWT | E. COLI NADH quinone oxidoreductase hydrophilic arm | electron microscopy | D | SF4 | — |
| 7Z7R | Complex I from E. coli, LMNG-purified, Apo, Open-ready state | electron microscopy | C | SF4, 3PE | — |
| 7Z7S | Complex I from E. coli, LMNG-purified, under Turnover at pH 6, Closed state | electron microscopy | C | SF4, 3PE, DCQ | 6 (best 0.88) |
| 7Z7T | Complex I from E. coli, LMNG-purified, under Turnover at pH 6, Open state | electron microscopy | C | SF4 | — |
| 7Z7V | Complex I from E. coli, LMNG-purified, under Turnover at pH 6, Open-ready state | electron microscopy | C | SF4, 3PE | 9 (best 0.89) |
| 7ZCI | Complex I from E. coli, LMNG-purified, under Turnover at pH 6, Resting state | electron microscopy | C | SF4 | 7 (best 0.87) |
Ligands
Elsewhere
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