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UniProt P15690

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (P15690)

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (UniProt P15690), EC 1.6.5.3, 1.6.99.3: 56 experimental structures and 1 predicted model on GenesisL1, 3 ligands bound, 121 pockets. Binding sites, druggability and…

UniProt
P15690
Protein
NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
EC
1.6.5.3, 1.6.99.3, 7.1.1.2
Experimental structures
56
Predicted models
1
Ligands
3
Pockets
121 · 41 records with a druggable one

Structures

57 records of P15690 in the MolNFT archive: 56 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory Complex I, class2electron microscopyGSF4, FES6 (best 0.89)
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopyGSF4, FES—
5LDWStructure of mammalian respiratory Complex I, class1electron microscopyGSF4, FES—
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopyGSF4, FES—
5LDXStructure of mammalian respiratory Complex I, class3.electron microscopyGSF4, FES5 (best 0.88)
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopyGSF4, FES—
5O31Mitochondrial complex I in the deactive stateelectron microscopyGSF4, FES4 (best 0.87)
5O31Mitochondrial complex I in the deactive stateelectron microscopyGSF4, FES—
7DGQActivity optimized supercomplex state1electron microscopyASF4, FES2 (best 0.85)
7DGRActivity optimized supercomplex state2electron microscopyASF4, FES3 (best 0.89)
7DGSActivity optimized supercomplex state3electron microscopyASF4, FES1 (best 0.88)
7DGZActivity optimized complex I (closed form)electron microscopyASF4, FES3 (best 0.88)
7DGZActivity optimized complex I (closed form)electron microscopyASF4, FES—
7DH0Activity optimized complex I (open form)electron microscopyASF4, FES2 (best 0.85)
7DH0Activity optimized complex I (open form)electron microscopyASF4, FES—
7DKFActivity optimized supercomplex state4electron microscopyA2SF4, FES2 (best 0.88)
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyGSF4, FES2 (best 0.89)
7QSDBovine complex I in the active state at 3.1 aelectron microscopyGSF4, FES—
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyGSF4, FES, K2 (best 0.90)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyGSF4, FES, K—
7QSLBovine complex I in lipid nanodisc, Active-apoelectron microscopyGSF4, FES, K3 (best 0.90)
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyGSF4, FES, K—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyGSF4, FES, K3 (best 0.90)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyGSF4, FES, K—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyGSF4, FES, K3 (best 0.90)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyGSF4, FES, K—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyGSF4, FES, K—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyGSF4, FES, K—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyGSF4, FES, K2 (best 0.90)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyGSF4, FES, K3 (best 0.88)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyGSF4, FES, K—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyGSF4, FES, K3 (best 0.89)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyGSF4, FES, K3 (best 0.90)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyGSF4, FES, K3 (best 0.90)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyGSF4, FES, K—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyGSF4, FES, K4 (best 0.88)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyGSF4, FES, K3 (best 0.90)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyGSF4, FES, K3 (best 0.89)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyGSF4, FES, K3 (best 0.89)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyGSF4, FES, K4 (best 0.90)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyGSF4, FES, K2 (best 0.89)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyGSF4, FES, K2 (best 0.89)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyGK, FES, SF42 (best 0.88)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyGSF4, FES, K4 (best 0.87)
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyGSF4, FES, K2 (best 0.89)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyGSF4, FES, K3 (best 0.89)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyGSF4, FES, K3 (best 0.86)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyGSF4, FES, K3 (best 0.88)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyGSF4, FES, K3 (best 0.86)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyGSF4, FES, K2 (best 0.88)
8Q45Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG.electron microscopyGSF4, FES, K3 (best 0.89)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyGSF4, FES, K3 (best 0.90)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyGSF4, FES, K3 (best 0.90)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyGSF4, FES, K2 (best 0.87)
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyGSF4, FES, K2 (best 0.90)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyGSF4, FES, K2 (best 0.88)
P15690AlphaFold monomer V2.0 prediction for NADH-ubiquinone oxidoreductase 75 kda subunit, mitochondrial…predictedA—8 (best 0.69)

Ligands

  • FES · Fe2/s2 (inorganic) cluster · in 56 records
  • SF4 · Iron/sulfur cluster · in 56 records
  • K · Potassium ion · in 38 records

Experiment against prediction

Elsewhere

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