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UniProt A0A1V3W1N5

NADH-quinone oxidoreductase subunit L (A0A1V3W1N5)

NADH-quinone oxidoreductase subunit L (UniProt A0A1V3W1N5), EC 1.6.5.11, 1.6.5.3: 12 experimental structures on GenesisL1, 2 ligands bound, 28 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
A0A1V3W1N5
Protein
NADH-quinone oxidoreductase subunit L
EC
1.6.5.11, 1.6.5.3, 1.6.99.5
Experimental structures
12
Predicted models
0
Ligands
2
Pockets
28 · 8 records with a druggable one

Structures

12 records of A0A1V3W1N5 in the MolNFT archive: 12 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
7NYHRespiratory complex I from Escherichia coli - focused refinement of membrane armelectron microscopyL—6 (best 0.83)
7NYHRespiratory complex I from escherichia COLI - focused refinement of membrane armelectron microscopyL——
7NYRRespiratory complex I from Escherichia coli - conformation 1electron microscopyL—4 (best 0.79)
7NYRRespiratory complex I from escherichia COLI - conformation 1electron microscopyL——
7NYURespiratory complex I from Escherichia coli - conformation 2electron microscopyL—3 (best 0.80)
7NYURespiratory complex I from escherichia COLI - conformation 2electron microscopyL——
7NYVRespiratory complex I from Escherichia coli - conformation 3electron microscopyL—3 (best 0.82)
7NYVRespiratory complex I from escherichia COLI - conformation 3electron microscopyL——
7Z80Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Closed stateelectron microscopyL3PE, LFA3 (best 0.79)
7Z83Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Open stateelectron microscopyL3PE3 (best 0.80)
7Z84Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Open-ready stateelectron microscopyL3PE, LFA3 (best 0.80)
7ZC5Complex I from E. coli, DDM/LMNG-purified, under Turnover at pH 8, Resting stateelectron microscopyL3PE, LFA3 (best 0.79)

Ligands

  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 4 records
  • LFA · Eicosane · in 3 records

Elsewhere

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