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UniProt Q05752

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 (Q05752)

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 (UniProt Q05752): 46 experimental structures and 1 predicted model on GenesisL1, 3 ligands bound, 20 pockets. Binding sites, druggability and experiment against…

UniProt
Q05752
Protein
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
Experimental structures
46
Predicted models
1
Ligands
3
Pockets
20 · 20 records with a druggable one

Structures

47 records of Q05752 in the MolNFT archive: 46 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5O31Mitochondrial complex I in the deactive stateelectron microscopyr—1 (best 0.83)
5O31Mitochondrial complex I in the deactive stateelectron microscopyr——
7DGQActivity optimized supercomplex state1electron microscopyPCDL—
7DGZActivity optimized complex I (closed form)electron microscopyPCDL—
7DGZActivity optimized complex I (closed form)electron microscopyPCDL—
7DH0Activity optimized complex I (open form)electron microscopyP——
7DH0Activity optimized complex I (open form)electron microscopyP——
7DKFActivity optimized supercomplex state4electron microscopyP2——
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyrCDL1 (best 0.89)
7QSDBovine complex I in the active state at 3.1 aelectron microscopyrCDL—
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyrPC1, CDL1 (best 0.90)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyrPC1, CDL—
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyr3PE, CDL—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyr3PE, CDL—
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyr3PE, CDL—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyr3PE, CDL1 (best 0.90)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyr3PE, CDL—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyr3PE, CDL—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyr3PE, CDL—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyrCDL1 (best 0.90)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyrCDL—
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyrCDL—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyrCDL—
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyrCDL—
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyr3PE, CDL1 (best 0.79)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyrCDL—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyrCDL1 (best 0.80)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyrCDL—
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyrCDL1 (best 0.79)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyr3PE, CDL1 (best 0.79)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyr3PE, CDL1 (best 0.81)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyr3PE, PC1, CDL—
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyrPC1, 3PE, CDL—
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyr3PE, CDL—
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyrPC1, 3PE, CDL1 (best 0.87)
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyr3PE, PC1, CDL1 (best 0.89)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyr3PE, CDL1 (best 0.81)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyr3PE, PC1, CDL—
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyr3PE, CDL1 (best 0.88)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyr3PE, PC1, CDL1 (best 0.86)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyrPC1, CDL, 3PE—
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyrPC1, 3PE, CDL1 (best 0.90)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyrPC1, 3PE, CDL1 (best 0.79)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyrPC1, 3PE, CDL1 (best 0.87)
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyrPC1, 3PE, CDL1 (best 0.90)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyrPC1, CDL, 3PE1 (best 0.88)
Q05752AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7…predictedA——

Ligands

  • CDL · Cardiolipin · in 41 records
  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 25 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 14 records

Experiment against prediction

Elsewhere

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