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UniProt Q7JAS9

NADH-ubiquinone oxidoreductase chain 3 (Q7JAS9)

NADH-ubiquinone oxidoreductase chain 3 (UniProt Q7JAS9), EC 7.1.1.2: 38 experimental structures on GenesisL1, 6 ligands bound, 88 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q7JAS9
Protein
NADH-ubiquinone oxidoreductase chain 3
EC
7.1.1.2
Experimental structures
38
Predicted models
0
Ligands
6
Pockets
88 · 29 records with a druggable one

Structures

38 records of Q7JAS9 in the MolNFT archive: 38 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyAPC1, 3PE2 (best 0.85)
7QSDBovine complex I in the active state at 3.1 aelectron microscopyAPC1, 3PE—
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyA3PE, PC1, U103 (best 0.87)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyA3PE, PC1—
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyA3PE, PC1—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyA3PE, PC13 (best 0.86)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyA3PE, PC1—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyAPC1, 3PE3 (best 0.88)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyAPC1, 3PE—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyA3PE, PC1—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyA3PE, PC1—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyAPC1, 3PE, CDL4 (best 0.87)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyAPC1, 3PE3 (best 0.92)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyAPC1, 3PE—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyAPC1, 3PE, CDL4 (best 0.90)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyA3PE, NDP3 (best 0.87)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyA3PE5 (best 0.89)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyA3PE, NDP—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyA3PE, NDP4 (best 0.89)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyA3PE, NDP3 (best 0.86)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyA3PE, NDP5 (best 0.89)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyAPC1, 3PE4 (best 0.88)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyA3PE2 (best 0.88)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyA3PE, PC1, PLC4 (best 0.88)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyA3PE, PC1, PLC2 (best 0.88)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyA3PE, PC13 (best 0.90)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyA3PE, PC1, PLC, CDL2 (best 0.86)
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyA3PE, PC1, PLC2 (best 0.88)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyA3PE, PC12 (best 0.90)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyA3PE, PC1, PLC2 (best 0.90)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyA3PE, PC1, PLC3 (best 0.86)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyA3PE, PC1, PLC3 (best 0.86)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyA3PE, PC1, CDL, PLC3 (best 0.87)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyA3PE, PC1, PLC2 (best 0.89)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyAPC1, 3PE, PLC4 (best 0.87)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyAPC1, 3PE, PLC, CDL2 (best 0.90)
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyAPC1, 3PE, PLC2 (best 0.87)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyA3PE, PC1, PLC, CDL4 (best 0.89)

Ligands

  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 38 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 31 records
  • PLC · Diundecyl phosphatidyl choline · in 13 records
  • CDL · Cardiolipin · in 6 records
  • NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · in 5 records
  • U10 · Ubiquinone-10 · in 1 record

Elsewhere

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