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UniProt E6BKM7

NADH-quinone oxidoreductase subunit H (E6BKM7)

NADH-quinone oxidoreductase subunit H (UniProt E6BKM7), EC 7.1.1.-: 8 experimental structures on GenesisL1, 3 ligands bound, 25 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
E6BKM7
Protein
NADH-quinone oxidoreductase subunit H
EC
7.1.1.-
Experimental structures
8
Predicted models
0
Ligands
3
Pockets
25 · 6 records with a druggable one

Structures

8 records of E6BKM7 in the MolNFT archive: 8 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
7Z7RComplex I from E. coli, LMNG-purified, Apo, Open-ready stateelectron microscopyH3PE, LFA—
7Z7SComplex I from E. coli, LMNG-purified, under Turnover at pH 6, Closed stateelectron microscopyH3PE, DCQ, LFA4 (best 0.88)
7Z7TComplex I from E. coli, LMNG-purified, under Turnover at pH 6, Open stateelectron microscopyH3PE, LFA—
7Z7VComplex I from E. coli, LMNG-purified, under Turnover at pH 6, Open-ready stateelectron microscopyH3PE, LFA4 (best 0.89)
7Z83Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Open stateelectron microscopyH3PE, LFA5 (best 0.81)
7Z84Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Open-ready stateelectron microscopyH3PE, LFA6 (best 0.88)
7ZC5Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Resting stateelectron microscopyHLFA, 3PE3 (best 0.73)
7ZCIComplex I from E. coli, LMNG-purified, under Turnover at pH 6, Resting stateelectron microscopyHLFA, 3PE3 (best 0.72)

Ligands

  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 8 records
  • LFA · Eicosane · in 8 records
  • DCQ · 2-decyl-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione · in 1 record

Elsewhere

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