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UniProt P23709

NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial (P23709)

NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial (UniProt P23709), EC 1.6.5.3, 1.6.99.3: 38 experimental structures and 1 predicted model on GenesisL1, 104 pockets. Binding sites, druggability and experiment…

UniProt
P23709
Protein
NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
EC
1.6.5.3, 1.6.99.3, 7.1.1.2
Experimental structures
38
Predicted models
1
Pockets
104 · 22 records with a druggable one

Structures

39 records of P23709 in the MolNFT archive: 38 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopyC——
5LDWStructure of mammalian respiratory Complex I, class1electron microscopyC——
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopyC——
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopyC——
5O31Mitochondrial complex I in the deactive stateelectron microscopyC—4 (best 0.87)
5O31Mitochondrial complex I in the deactive stateelectron microscopyC——
7DGQActivity optimized supercomplex state1electron microscopyC—2 (best 0.85)
7DGZActivity optimized complex I (closed form)electron microscopyC——
7DH0Activity optimized complex I (open form)electron microscopyC——
7DKFActivity optimized supercomplex state4electron microscopyC2—2 (best 0.88)
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyC—4 (best 0.89)
7QSDBovine complex I in the active state at 3.1 aelectron microscopyC——
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyC——
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyC——
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyC—4 (best 0.90)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyC——
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyC——
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyC——
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyC——
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyC—5 (best 0.90)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyC——
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyC—6 (best 0.89)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyC—5 (best 0.90)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyC—5 (best 0.90)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyC——
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyC—5 (best 0.88)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyC—5 (best 0.90)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyC—5 (best 0.90)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyC—4 (best 0.89)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyC—5 (best 0.89)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyC—5 (best 0.88)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyC—6 (best 0.87)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyC—6 (best 0.88)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyC—4 (best 0.88)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyC—5 (best 0.86)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyC—5 (best 0.90)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyC—6 (best 0.90)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyC—6 (best 0.88)
P23709AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] iron-sulfur protein 3…predictedA——

Experiment against prediction

Elsewhere

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