GL1X · GenesisL1 explorer

UniProt Q02378

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 (Q02378)

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 (UniProt Q02378): 53 experimental structures and 1 predicted model on GenesisL1, 4 ligands bound, 26 pockets. Binding sites, druggability and experiment against…

UniProt
Q02378
Protein
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
Experimental structures
53
Predicted models
1
Ligands
4
Pockets
26 · 24 records with a druggable one

Structures

54 records of Q02378 in the MolNFT archive: 53 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory Complex I, class2electron microscopyf—1 (best 0.84)
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopyf——
5LDWStructure of mammalian respiratory Complex I, class1electron microscopyf——
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopyf——
5LDXStructure of mammalian respiratory Complex I, class3.electron microscopyf—1 (best 0.80)
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopyf——
5O31Mitochondrial complex I in the deactive stateelectron microscopyf—1 (best 0.84)
5O31Mitochondrial complex I in the deactive stateelectron microscopyf——
7DGQActivity optimized supercomplex state1electron microscopyXPC1—
7DGZActivity optimized complex I (closed form)electron microscopyX—1 (best 0.82)
7DGZActivity optimized complex I (closed form)electron microscopyX——
7DH0Activity optimized complex I (open form)electron microscopyX——
7DH0Activity optimized complex I (open form)electron microscopyX——
7DKFActivity optimized supercomplex state4electron microscopyX2——
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyf3PE—
7QSDBovine complex I in the active state at 3.1 aelectron microscopyf3PE—
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyfCDL1 (best 0.86)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyfCDL—
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyfCDL—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyfCDL, 3PE2 (best 0.85)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyfCDL, 3PE—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyfCDL, 3PE1 (best 0.83)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyfCDL, 3PE—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyfCDL—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyfCDL—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyf3PE1 (best 0.82)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyf3PE1 (best 0.83)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyf3PE—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyf3PE1 (best 0.80)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyfCDL1 (best 0.84)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyfCDL—
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyfCDL—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyfCDL1 (best 0.83)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyfCDL1 (best 0.84)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyfCDL—
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyfCDL2 (best 0.87)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyfCDL1 (best 0.80)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyf3PE, CDL, PLC1 (best 0.83)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyfPLC, CDL, 3PE—
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyfCDL1 (best 0.79)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyfPLC, CDL, 3PE—
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyf3PE, PLC, CDL1 (best 0.84)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyfCDL—
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyfPLC, CDL, 3PE—
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyfCDL, 3PE—
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyf3PE, CDL, PLC1 (best 0.84)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyfPLC, CDL, 3PE—
8Q45Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG.electron microscopyfCDL, PLC, 3PE1 (best 0.84)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyfPLC, CDL, 3PE1 (best 0.85)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyfCDL, 3PE1 (best 0.84)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyf3PE, PLC, CDL—
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyfCDL, PLC, 3PE1 (best 0.85)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyf3PE, PLC, CDL1 (best 0.86)
Q02378AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1…predictedA——

Ligands

  • CDL · Cardiolipin · in 33 records
  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 24 records
  • PLC · Diundecyl phosphatidyl choline · in 12 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 1 record

Experiment against prediction

Elsewhere

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