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UniProt Q02375

NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial (Q02375)

NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial (UniProt Q02375): 46 experimental structures and 1 predicted model on GenesisL1, 1 ligand bound, 125 pockets. Binding sites, druggability and experiment against…

UniProt
Q02375
Protein
NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
Experimental structures
46
Predicted models
1
Ligands
1
Pockets
125 · 34 records with a druggable one

Structures

47 records of Q02375 in the MolNFT archive: 46 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5O31Mitochondrial complex I in the deactive stateelectron microscopyQ—3 (best 0.87)
5O31Mitochondrial complex I in the deactive stateelectron microscopyQ——
7DGQActivity optimized supercomplex state1electron microscopyG—2 (best 0.85)
7DGZActivity optimized complex I (closed form)electron microscopyG—3 (best 0.88)
7DGZActivity optimized complex I (closed form)electron microscopyG——
7DH0Activity optimized complex I (open form)electron microscopyG—2 (best 0.84)
7DH0Activity optimized complex I (open form)electron microscopyG——
7DKFActivity optimized supercomplex state4electron microscopyG2—2 (best 0.88)
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyQ—3 (best 0.89)
7QSDBovine complex I in the active state at 3.1 aelectron microscopyQ——
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyQ—3 (best 0.90)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyQ——
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyQ——
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyQ—3 (best 0.90)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyQ——
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyQ—4 (best 0.90)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyQ——
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyQ——
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyQ——
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyQ—3 (best 0.90)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyQ—5 (best 0.88)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyQK—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyQK4 (best 0.89)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyQK4 (best 0.90)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyQ—4 (best 0.90)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyQ——
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyQ—4 (best 0.88)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyQ—4 (best 0.90)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyQK4 (best 0.89)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyQK4 (best 0.89)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyQ—5 (best 0.90)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyQ—3 (best 0.89)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyQK4 (best 0.89)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyQ—3 (best 0.88)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyQK5 (best 0.87)
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyQ—4 (best 0.89)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyQK4 (best 0.89)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyQ—5 (best 0.87)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyQK3 (best 0.88)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyQ—4 (best 0.86)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyQ—4 (best 0.88)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyQK4 (best 0.90)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyQK4 (best 0.90)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyQK4 (best 0.87)
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyQK4 (best 0.90)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyQK4 (best 0.88)
Q02375AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] iron-sulfur protein 4…predictedA——

Ligands

  • K · Potassium ion · in 14 records

Experiment against prediction

Elsewhere

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