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UniProt P42029

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 (P42029)

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 (UniProt P42029): 56 experimental structures and 1 predicted model on GenesisL1, 3 ligands bound, 179 pockets. Binding sites, druggability and experiment against…

UniProt
P42029
Protein
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
Experimental structures
56
Predicted models
1
Ligands
3
Pockets
179 · 40 records with a druggable one

Structures

57 records of P42029 in the MolNFT archive: 56 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory Complex I, class2electron microscopyX—2 (best 0.90)
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopyX——
5LDWStructure of mammalian respiratory Complex I, class1electron microscopyX——
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopyX——
5LDXStructure of mammalian respiratory Complex I, class3.electron microscopyX—4 (best 0.88)
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopyX——
5O31Mitochondrial complex I in the deactive stateelectron microscopyX—3 (best 0.88)
5O31Mitochondrial complex I in the deactive stateelectron microscopyX——
7DGQActivity optimized supercomplex state1electron microscopyQPC12 (best 0.85)
7DGRActivity optimized supercomplex state2electron microscopyQPC11 (best 0.88)
7DGSActivity optimized supercomplex state3electron microscopyQPC13 (best 0.90)
7DGZActivity optimized complex I (closed form)electron microscopyQPC13 (best 0.89)
7DGZActivity optimized complex I (closed form)electron microscopyQPC1—
7DH0Activity optimized complex I (open form)electron microscopyQ—4 (best 0.88)
7DH0Activity optimized complex I (open form)electron microscopyQ——
7DKFActivity optimized supercomplex state4electron microscopyQ2—3 (best 0.89)
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyX3PE6 (best 0.86)
7QSDBovine complex I in the active state at 3.1 aelectron microscopyX3PE—
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyXCDL5 (best 0.86)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyXCDL—
7QSLBovine complex I in lipid nanodisc, Active-apoelectron microscopyXCDL5 (best 0.91)
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyXCDL—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyXCDL6 (best 0.86)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyXCDL—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyXCDL6 (best 0.86)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyXCDL—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyXCDL—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyXCDL—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyX3PE4 (best 0.86)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyX3PE4 (best 0.92)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyX3PE—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyX3PE4 (best 0.90)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyXCDL6 (best 0.86)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyXCDL4 (best 0.89)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyXCDL—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyXCDL5 (best 0.89)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyXCDL6 (best 0.86)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyXCDL4 (best 0.89)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyXCDL5 (best 0.87)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyXCDL3 (best 0.88)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyXCDL5 (best 0.86)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyXCDL5 (best 0.86)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyXCDL4 (best 0.90)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyXCDL3 (best 0.85)
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyXCDL5 (best 0.86)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyXCDL4 (best 0.90)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyXCDL4 (best 0.90)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyXCDL5 (best 0.86)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyXCDL6 (best 0.86)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyXCDL4 (best 0.85)
8Q45Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG.electron microscopyXCDL6 (best 0.86)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyXCDL5 (best 0.89)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyXCDL5 (best 0.86)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyXCDL5 (best 0.90)
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyXCDL7 (best 0.86)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyXCDL7 (best 0.87)
P42029AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8…predictedA—1 (best 0.29)

Ligands

  • CDL · Cardiolipin · in 34 records
  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 6 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 5 records

Experiment against prediction

Elsewhere

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