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UniProt Q8HXG6

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 (Q8HXG6)

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 (UniProt Q8HXG6): 54 experimental structures and 1 predicted model on GenesisL1, 5 ligands bound, 18 pockets. Binding sites, druggability and experiment against…

UniProt
Q8HXG6
Protein
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
Experimental structures
54
Predicted models
1
Ligands
5
Pockets
18 · 17 records with a druggable one

Structures

55 records of Q8HXG6 in the MolNFT archive: 54 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory Complex I, class2electron microscopyY—2 (best 0.86)
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopyY——
5LDWStructure of mammalian respiratory Complex I, class1electron microscopyY——
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopyY——
5LDXStructure of mammalian respiratory Complex I, class3.electron microscopyY—1 (best 0.83)
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopyY——
5O31Mitochondrial complex I in the deactive stateelectron microscopyY—1 (best 0.84)
5O31Mitochondrial complex I in the deactive stateelectron microscopyY——
7DGQActivity optimized supercomplex state1electron microscopyT3PE—
7DGRActivity optimized supercomplex state2electron microscopyT3PE—
7DGZActivity optimized complex I (closed form)electron microscopyT3PE1 (best 0.84)
7DGZActivity optimized complex I (closed form)electron microscopyT3PE—
7DH0Activity optimized complex I (open form)electron microscopyT3PE1 (best 0.85)
7DH0Activity optimized complex I (open form)electron microscopyT3PE—
7DKFActivity optimized supercomplex state4electron microscopyT23PE1 (best 0.85)
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyY3PE, CDL—
7QSDBovine complex I in the active state at 3.1 aelectron microscopyY3PE, CDL—
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyY3PE, PC1—
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyY3PE, PC1—
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyYCDL, 3PE, PC1—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyY3PE, PC1—
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyY3PE, PC1—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyY3PE, PC1—
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyY3PE, PC1—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyY3PE—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyY3PE—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyYCDL, 3PE, I491 (best 0.81)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyYCDL, 3PE, I491 (best 0.80)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyYCDL, 3PE—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyYCDL, 3PE—
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyYCDL, 3PE, I491 (best 0.80)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyYCDL, 3PE1 (best 0.81)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyYCDL, 3PE, I49—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyYCDL, 3PE, I491 (best 0.81)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyY3PE, I49, CDL1 (best 0.82)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyYI49, 3PE1 (best 0.81)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyYI49, 3PE1 (best 0.82)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyY3PE, I491 (best 0.81)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyY3PE, PC1—
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyY3PE, PC1, PLC—
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyY3PE1 (best 0.80)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyY3PE, PC1, PLC—
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyY3PE, PC1, PLC—
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyY3PE—
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyY3PE, PC1, PLC—
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyY3PE, PC1—
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyY3PE, PC1, PLC—
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyY3PE, PC1, PLC—
8Q45Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG.electron microscopyY3PE, PC1, PLC—
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyY3PE, PC1, PLC—
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyY3PE, PC1—
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyY3PE, PC1, PLC—
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyY3PE, PC1, PLC—
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyY3PE, PC1, PLC—
Q8HXG6AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11…predictedA—1 (best 0.51)

Ligands

  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 46 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 21 records
  • CDL · Cardiolipin · in 12 records
  • PLC · Diundecyl phosphatidyl choline · in 11 records
  • I49 · 1-carbamimidoyl-3-[2-(3-chloranyl-4-iodanyl-phenyl)ethyl]guanidine · in 9 records

Experiment against prediction

Elsewhere

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