UniProt A0A0H3MIP2
NADH-quinone oxidoreductase subunit J (A0A0H3MIP2)
NADH-quinone oxidoreductase subunit J (UniProt A0A0H3MIP2), EC 7.1.1.-: 9 experimental structures on GenesisL1, 2 ligands bound, 16 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- A0A0H3MIP2
- Protein
- NADH-quinone oxidoreductase subunit J
- EC
- 7.1.1.-
- Experimental structures
- 9
- Predicted models
- 0
- Ligands
- 2
- Pockets
- 16 · 7 records with a druggable one
Structures
9 records of A0A0H3MIP2 in the MolNFT archive: 9 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 7Z7R | Complex I from E. coli, LMNG-purified, Apo, Open-ready state | electron microscopy | J | — | — |
| 7Z7S | Complex I from E. coli, LMNG-purified, under Turnover at pH 6, Closed state | electron microscopy | J | 3PE, LFA | 3 (best 0.75) |
| 7Z7T | Complex I from E. coli, LMNG-purified, under Turnover at pH 6, Open state | electron microscopy | J | 3PE | — |
| 7Z7V | Complex I from E. coli, LMNG-purified, under Turnover at pH 6, Open-ready state | electron microscopy | J | 3PE, LFA | 3 (best 0.89) |
| 7Z80 | Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Closed state | electron microscopy | J | LFA, 3PE | 2 (best 0.69) |
| 7Z83 | Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Open state | electron microscopy | J | 3PE | 3 (best 0.78) |
| 7Z84 | Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Open-ready state | electron microscopy | J | LFA, 3PE | 2 (best 0.71) |
| 7ZC5 | Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Resting state | electron microscopy | J | LFA, 3PE | 2 (best 0.72) |
| 7ZCI | Complex I from E. coli, LMNG-purified, under Turnover at pH 6, Resting state | electron microscopy | J | 3PE, LFA | 1 (best 0.72) |
Ligands
Elsewhere
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