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UniProt E2QPD7

NADH-quinone oxidoreductase subunit N (E2QPD7)

NADH-quinone oxidoreductase subunit N (UniProt E2QPD7), EC 7.1.1.-: 9 experimental structures on GenesisL1, 3 ligands bound, 31 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
E2QPD7
Protein
NADH-quinone oxidoreductase subunit N
EC
7.1.1.-
Experimental structures
9
Predicted models
0
Ligands
3
Pockets
31 · 9 records with a druggable one

Structures

9 records of E2QPD7 in the MolNFT archive: 9 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
7Z7RComplex I from E. coli, LMNG-purified, Apo, Open-ready stateelectron microscopyN—2 (best 0.77)
7Z7SComplex I from E. coli, LMNG-purified, under Turnover at pH 6, Closed stateelectron microscopyN3PE, LFA4 (best 0.76)
7Z7TComplex I from E. coli, LMNG-purified, under Turnover at pH 6, Open stateelectron microscopyN3PE, LFA3 (best 0.77)
7Z7VComplex I from E. coli, LMNG-purified, under Turnover at pH 6, Open-ready stateelectron microscopyN3PE, C143 (best 0.74)
7Z80Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Closed stateelectron microscopyN3PE, LFA4 (best 0.74)
7Z83Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Open stateelectron microscopyN3PE, LFA4 (best 0.76)
7Z84Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Open-ready stateelectron microscopyN3PE, LFA3 (best 0.74)
7ZC5Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Resting stateelectron microscopyNLFA, 3PE5 (best 0.74)
7ZCIComplex I from E. coli, LMNG-purified, under Turnover at pH 6, Resting stateelectron microscopyNLFA, 3PE3 (best 0.76)

Ligands

  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 8 records
  • LFA · Eicosane · in 7 records
  • C14 · Tetradecane · in 1 record

Elsewhere

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