GL1X · GenesisL1 explorer

UniProt P03887

NADH-ubiquinone oxidoreductase chain 1 (P03887)

NADH-ubiquinone oxidoreductase chain 1 (UniProt P03887), EC 1.6.5.3, 7.1.1.2: 52 experimental structures and 1 predicted model on GenesisL1, 7 ligands bound, 149 pockets. Binding sites, druggability and experiment against…

UniProt
P03887
Protein
NADH-ubiquinone oxidoreductase chain 1
EC
1.6.5.3, 7.1.1.2
Experimental structures
52
Predicted models
1
Ligands
7
Pockets
149 · 37 records with a druggable one

Structures

53 records of P03887 in the MolNFT archive: 52 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory Complex I, class2electron microscopyH—3 (best 0.90)
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopyH——
5LDWStructure of mammalian respiratory Complex I, class1electron microscopyH——
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopyH——
5LDXStructure of mammalian respiratory Complex I, class3.electron microscopyH—3 (best 0.88)
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopyH——
5O31Mitochondrial complex I in the deactive stateelectron microscopyH—2 (best 0.88)
5O31Mitochondrial complex I in the deactive stateelectron microscopyH——
7DGQActivity optimized supercomplex state1electron microscopy1PC1, 3PE3 (best 0.86)
7DGZActivity optimized complex I (closed form)electron microscopy13PE, PC13 (best 0.89)
7DGZActivity optimized complex I (closed form)electron microscopy13PE, PC1—
7DH0Activity optimized complex I (open form)electron microscopy13PE3 (best 0.87)
7DH0Activity optimized complex I (open form)electron microscopy13PE—
7DKFActivity optimized supercomplex state4electron microscopy123PE2 (best 0.89)
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyH3PE, PC1, CDL4 (best 0.89)
7QSDBovine complex I in the active state at 3.1 aelectron microscopyH3PE, PC1, CDL—
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyH3PE, PC1, U10, CDL4 (best 0.87)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyH3PE, PC1, U10, CDL—
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyHPC1, 3PE, CDL—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyH3PE, PC1, CDL4 (best 0.86)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyH3PE, PC1, CDL—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyHPC1, 3PE, CDL3 (best 0.88)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyHPC1, 3PE, CDL—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyH3PE, PC1, CHD, CDL—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyH3PE, PC1, CHD, CDL—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyHPC1, 3PE, CDL5 (best 0.87)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyHPC1, 3PE, CDL3 (best 0.92)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyHPC1, 3PE, CDL—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyHPC1, 3PE, CDL5 (best 0.90)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyHPC1, 3PE, I49, CDL4 (best 0.87)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyH3PE, PC1, I49, CDL7 (best 0.89)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyH3PE, I49, PC1, CDL—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyH3PE, PC1, I49, CDL5 (best 0.89)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyHPC1, 3PE, I49, CDL4 (best 0.86)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyH3PE, PC1, CDL6 (best 0.89)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyHPC1, 3PE, CDL5 (best 0.88)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyH3PE, PC1, I49, CDL3 (best 0.88)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyH3PE, PC1, CDL4 (best 0.88)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyH3PE, PC1, PLC, CDL4 (best 0.86)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyH3PE, PC1, CDL4 (best 0.90)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyH3PE, PC1, U10, CDL, PLC4 (best 0.89)
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyHPC1, 3PE, CDL5 (best 0.88)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyH3PE, PC1, CDL3 (best 0.90)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyH3PE, PC1, PLC, CDL5 (best 0.90)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyHPC1, U10, CDL, 3PE5 (best 0.86)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyH3PE, PC1, CDL3 (best 0.86)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyHPC1, U10, CDL, PLC, 3PE5 (best 0.87)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyH3PE, PC1, PLC, CDL5 (best 0.89)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyHPC1, U10, CDL, 3PE6 (best 0.87)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyHPC1, 3PE, U10, CDL, PLC3 (best 0.90)
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyH3PE, PC1, CDL4 (best 0.87)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyH3PE, PC1, U10, CDL, PLC5 (best 0.89)
P03887AlphaFold monomer V2.0 prediction for NADH-ubiquinone oxidoreductase chain 1 (P03887)predictedA—3 (best 0.79)

Ligands

  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 44 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 41 records
  • CDL · Cardiolipin · in 38 records
  • U10 · Ubiquinone-10 · in 8 records
  • PLC · Diundecyl phosphatidyl choline · in 7 records
  • I49 · 1-carbamimidoyl-3-[2-(3-chloranyl-4-iodanyl-phenyl)ethyl]guanidine · in 6 records
  • CHD · Cholic acid · in 2 records

Experiment against prediction

Elsewhere

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.