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UniProt P48305

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 (P48305)

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 (UniProt P48305): 54 experimental structures and 1 predicted model on GenesisL1, 2 ligands bound, 72 pockets. Binding sites, druggability and experiment against…

UniProt
P48305
Protein
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
Experimental structures
54
Predicted models
1
Ligands
2
Pockets
72 · 37 records with a druggable one

Structures

55 records of P48305 in the MolNFT archive: 54 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory Complex I, class2electron microscopym—2 (best 0.84)
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopym——
5LDWStructure of mammalian respiratory Complex I, class1electron microscopym——
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopym——
5LDXStructure of mammalian respiratory Complex I, class3.electron microscopym—2 (best 0.86)
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopym——
5O31Mitochondrial complex I in the deactive stateelectron microscopym—1 (best 0.83)
5O31Mitochondrial complex I in the deactive stateelectron microscopym——
7DGQActivity optimized supercomplex state1electron microscopya—2 (best 0.87)
7DGRActivity optimized supercomplex state2electron microscopya—1 (best 0.88)
7DGZActivity optimized complex I (closed form)electron microscopya—3 (best 0.90)
7DGZActivity optimized complex I (closed form)electron microscopya——
7DH0Activity optimized complex I (open form)electron microscopya—2 (best 0.86)
7DH0Activity optimized complex I (open form)electron microscopya——
7DKFActivity optimized supercomplex state4electron microscopya2—2 (best 0.90)
7QSDBovine complex I in the active state at 3.1 Aelectron microscopym—2 (best 0.87)
7QSDBovine complex I in the active state at 3.1 aelectron microscopym——
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopym3PE, PC13 (best 0.86)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopym3PE, PC1—
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopym3PE, PC1—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopym3PE1 (best 0.84)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopym3PE—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopym3PE, PC12 (best 0.87)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopym3PE, PC1—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopym——
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopym——
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopym—2 (best 0.85)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopym—2 (best 0.87)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopym——
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopym—3 (best 0.86)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopym—2 (best 0.84)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopym—1 (best 0.84)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopym——
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopym3PE1 (best 0.85)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopym—2 (best 0.85)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopym—2 (best 0.85)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopym—1 (best 0.83)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopym—1 (best 0.84)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopymPC1, 3PE2 (best 0.87)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopym3PE, PC13 (best 0.87)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopym—2 (best 0.86)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopym3PE, PC11 (best 0.86)
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopym3PE, PC12 (best 0.86)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopym——
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopym3PE, PC12 (best 0.87)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopym3PE, PC13 (best 0.86)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopym3PE, PC12 (best 0.88)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopym3PE, PC11 (best 0.88)
8Q45Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG.electron microscopym3PE, PC12 (best 0.87)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopym3PE, PC13 (best 0.86)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopym3PE, PC13 (best 0.87)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopym3PE, PC12 (best 0.87)
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopym3PE, PC12 (best 0.87)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopym3PE, PC12 (best 0.87)
P48305AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4…predictedA——

Ligands

  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 22 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 19 records

Experiment against prediction

Elsewhere

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