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UniProt Q8HXG5

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial (Q8HXG5)

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial (UniProt Q8HXG5): 36 experimental structures and 1 predicted model on GenesisL1, 5 ligands bound, 51 pockets. Binding sites, druggability and experiment…

UniProt
Q8HXG5
Protein
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial
Experimental structures
36
Predicted models
1
Ligands
5
Pockets
51 · 20 records with a druggable one

Structures

37 records of Q8HXG5 in the MolNFT archive: 36 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopyg——
5LDWStructure of mammalian respiratory Complex I, class1electron microscopyg——
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopyg——
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopyg——
5O31Mitochondrial complex I in the deactive stateelectron microscopyg—3 (best 0.87)
5O31Mitochondrial complex I in the deactive stateelectron microscopyg——
7DGQActivity optimized supercomplex state1electron microscopyhCDL2 (best 0.87)
7DGZActivity optimized complex I (closed form)electron microscopyhCDL—
7DH0Activity optimized complex I (open form)electron microscopyhCDL—
7DKFActivity optimized supercomplex state4electron microscopyh2CDL1 (best 0.90)
7QSDBovine complex I in the active state at 3.1 Aelectron microscopygPC1, CDL2 (best 0.87)
7QSDBovine complex I in the active state at 3.1 aelectron microscopygPC1, CDL—
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopygPC1, CDL—
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopygPC1, CDL—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopygCDL, PC1, 3PE2 (best 0.85)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopygCDL, PC1, 3PE—
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopygPC1, 3PE, CDL—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopygCDL, PC1—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopygCDL, PC1—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopygCDL, PC14 (best 0.86)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopygCDL, PC1—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopygCDL, 3PE, PC14 (best 0.83)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopygCDL, PC13 (best 0.85)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopygCDL, PC12 (best 0.85)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopygCDL, PC1—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopygCDL, PC13 (best 0.85)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopygCDL, PC12 (best 0.84)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopygCDL, PC13 (best 0.83)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopygCDL, ZN, 3PE, PC1, PLC3 (best 0.84)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopygCDL, ZN, PC1, 3PE, PLC2 (best 0.85)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyg—2 (best 0.85)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopygPC1, CDL, ZN, 3PE, PLC2 (best 0.84)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopygCDL, 3PE, PC1, PLC2 (best 0.85)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopygCDL, ZN, PC1, 3PE, PLC3 (best 0.85)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopygZN, 3PE, PC1, PLC, CDL3 (best 0.85)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopygCDL, PC1, ZN, 3PE, PLC3 (best 0.85)
Q8HXG5AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11…predictedA——

Ligands

  • CDL · Cardiolipin · in 29 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 25 records
  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 11 records
  • PLC · Diundecyl phosphatidyl choline · in 7 records
  • ZN · Zinc ion · in 6 records

Experiment against prediction

Elsewhere

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