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UniProt P42028

NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial (P42028)

NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial (UniProt P42028), EC 1.6.5.3, 1.6.99.3: 55 experimental structures and 1 predicted model on GenesisL1, 4 ligands bound, 98 pockets. Binding sites, druggability…

UniProt
P42028
Protein
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
EC
1.6.5.3, 1.6.99.3, 7.1.1.2
Experimental structures
55
Predicted models
1
Ligands
4
Pockets
98 · 36 records with a druggable one

Structures

56 records of P42028 in the MolNFT archive: 55 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory Complex I, class2electron microscopyISF44 (best 0.84)
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopyISF4—
5LDWStructure of mammalian respiratory Complex I, class1electron microscopyISF4—
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopyISF4—
5LDXStructure of mammalian respiratory Complex I, class3.electron microscopyISF41 (best 0.87)
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopyISF4—
5O31Mitochondrial complex I in the deactive stateelectron microscopyISF44 (best 0.87)
5O31Mitochondrial complex I in the deactive stateelectron microscopyISF4—
7DGQActivity optimized supercomplex state1electron microscopyE3PE, SF4, CDL1 (best 0.85)
7DGRActivity optimized supercomplex state2electron microscopyE3PE, SF4, CDL2 (best 0.86)
7DGSActivity optimized supercomplex state3electron microscopyE3PE, SF4—
7DGZActivity optimized complex I (closed form)electron microscopyE3PE, SF4—
7DGZActivity optimized complex I (closed form)electron microscopyE3PE, SF4—
7DH0Activity optimized complex I (open form)electron microscopyE3PE, SF42 (best 0.86)
7DH0Activity optimized complex I (open form)electron microscopyE3PE, SF4—
7DKFActivity optimized supercomplex state4electron microscopyE23PE, SF4—
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyIPC1, 3PE, SF4, CDL2 (best 0.89)
7QSDBovine complex I in the active state at 3.1 aelectron microscopyI3PE, SF4—
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyIPC1, SF42 (best 0.90)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyIPC1, SF4—
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyI3PE, SF4, CDL—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyIPC1, 3PE, SF42 (best 0.90)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyI3PE, SF4—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyI3PE, SF4, CDL2 (best 0.84)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyI3PE, SF4, CDL—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyI3PE, SF4—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyI3PE, SF4—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyIPC1, 3PE, SF4, CDL2 (best 0.90)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyIPC1, 3PE, SF4, CDL3 (best 0.88)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyI3PE, SF4, CDL—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyIPC1, 3PE, SF4, CDL3 (best 0.89)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyIPC1, 3PE, SF4, CDL3 (best 0.90)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyIPC1, 3PE, SF4, CDL4 (best 0.90)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyI3PE, SF4, CDL—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyI3PE, SF4, CDL4 (best 0.88)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyIPC1, 3PE, SF43 (best 0.90)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyIPC1, 3PE, SF4, CDL3 (best 0.84)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyIPC1, 3PE, SF4, CDL4 (best 0.89)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyIPC1, 3PE, SF4, CDL3 (best 0.90)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyIPC1, SF4, 3PE2 (best 0.89)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyIPC1, SF4, 3PE3 (best 0.89)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyIPC1, 3PE, SF41 (best 0.84)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyIPC1, SF4, 3PE3 (best 0.87)
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyIPC1, SF4, 3PE3 (best 0.89)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyI3PE, SF44 (best 0.89)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyIPC1, SF4, 3PE3 (best 0.84)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyIPC1, SF4, 3PE2 (best 0.88)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyIPC1, SF4, 3PE2 (best 0.86)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyIPC1, SF4, 3PE3 (best 0.88)
8Q45Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG.electron microscopyIPC1, SF4, 3PE2 (best 0.89)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyIPC1, SF4, 3PE3 (best 0.90)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyIPC1, SF4, 3PE4 (best 0.90)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyIPC1, SF4, 3PE3 (best 0.87)
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyIPC1, SF4, 3PE3 (best 0.90)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyIPC1, SF4, 3PE3 (best 0.88)
P42028AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] iron-sulfur protein 8…predictedA——

Ligands

  • SF4 · Iron/sulfur cluster · in 55 records
  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 45 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 28 records
  • CDL · Cardiolipin · in 17 records

Experiment against prediction

Elsewhere

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