GL1X · GenesisL1 explorer

UniProt Q02366

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 (Q02366)

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 (UniProt Q02366): 54 experimental structures and 1 predicted model on GenesisL1, 1 ligand bound, 117 pockets. Binding sites, druggability and experiment against…

UniProt
Q02366
Protein
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
Experimental structures
54
Predicted models
1
Ligands
1
Pockets
117 · 39 records with a druggable one

Structures

55 records of Q02366 in the MolNFT archive: 54 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5LC5Structure of mammalian respiratory Complex I, class2electron microscopyW—1 (best 0.87)
5LC5Structure of mammalian respiratory complex I, CLASS2electron microscopyW——
5LDWStructure of mammalian respiratory Complex I, class1electron microscopyW——
5LDWStructure of mammalian respiratory complex I, CLASS1electron microscopyW——
5LDXStructure of mammalian respiratory Complex I, class3.electron microscopyW—1 (best 0.83)
5LDXStructure of mammalian respiratory complex I, CLASS3.electron microscopyW——
5O31Mitochondrial complex I in the deactive stateelectron microscopyW—2 (best 0.87)
5O31Mitochondrial complex I in the deactive stateelectron microscopyW——
7DGQActivity optimized supercomplex state1electron microscopyO—1 (best 0.85)
7DGRActivity optimized supercomplex state2electron microscopyO—3 (best 0.87)
7DGZActivity optimized complex I (closed form)electron microscopyO—3 (best 0.88)
7DGZActivity optimized complex I (closed form)electron microscopyO——
7DH0Activity optimized complex I (open form)electron microscopyO—2 (best 0.84)
7DH0Activity optimized complex I (open form)electron microscopyO——
7DKFActivity optimized supercomplex state4electron microscopyO2—2 (best 0.88)
7QSDBovine complex I in the active state at 3.1 Aelectron microscopyWEHZ3 (best 0.87)
7QSDBovine complex I in the active state at 3.1 aelectron microscopyWEHZ—
7QSKBovine complex I in lipid nanodisc, Active-Q10electron microscopyWEHZ3 (best 0.90)
7QSKBovine complex I in lipid nanodisc, active-Q10electron microscopyWEHZ—
7QSLBovine complex I in lipid nanodisc, active-apoelectron microscopyWEHZ—
7QSMBovine complex I in lipid nanodisc, Deactive-ligand (composite)electron microscopyWEHZ3 (best 0.90)
7QSMBovine complex I in lipid nanodisc, deactive-ligand (composite)electron microscopyWEHZ—
7QSNBovine complex I in lipid nanodisc, Deactive-apoelectron microscopyWEHZ4 (best 0.90)
7QSNBovine complex I in lipid nanodisc, deactive-apoelectron microscopyWEHZ—
7QSOBovine complex I in lipid nanodisc, State 3 (Slack)electron microscopyWEHZ—
7QSOBovine complex I in lipid nanodisc, state 3 (slack)electron microscopyWEHZ—
7R41Bovine complex I in the presence of IM1761092, active class i (Composite map)electron microscopyWEHZ4 (best 0.90)
7R42Bovine complex I in the presence of IM1761092, active class ii (Composite map)electron microscopyWEHZ4 (best 0.84)
7R43Bovine complex I in the presence of IM1761092, active class iii (Composite map)electron microscopyWEHZ—
7R44Bovine complex I in the presence of IM1761092, active class iv (Composite map)electron microscopyWEHZ4 (best 0.89)
7R45Bovine complex I in the presence of IM1761092, deactive class i (Composite map)electron microscopyWEHZ3 (best 0.90)
7R46Bovine complex I in the presence of IM1761092, deactive class ii (Composite map)electron microscopyWEHZ3 (best 0.90)
7R47Bovine complex I in the presence of IM1761092, deactive class iii (Composite map)electron microscopyWEHZ—
7R48Bovine complex I in the presence of IM1761092, deactive class iv (Composite map)electron microscopyWEHZ2 (best 0.87)
7R4CBovine complex I in the presence of IM1761092, deactive class v (Composite map)electron microscopyWEHZ3 (best 0.90)
7R4DBovine complex I in the presence of IM1761092, deactive class vi (Composite map)electron microscopyWEHZ3 (best 0.89)
7R4FBovine complex I in the presence of IM1761092, slack class i (Composite map)electron microscopyWEHZ4 (best 0.89)
7R4GBovine complex I in the presence of IM1761092, slack class ii (Composite map)electron microscopyWEHZ3 (best 0.90)
8Q0AInward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyWEHZ4 (best 0.89)
8Q0FInward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyWEHZ4 (best 0.89)
8Q0JInward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.electron microscopyWEHZ3 (best 0.88)
8Q0MOutward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyWEHZ4 (best 0.86)
8Q0OOutward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.electron microscopyWEHZ3 (best 0.88)
8Q0QOutward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDMelectron microscopyWEHZ3 (best 0.84)
8Q1PInward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially…electron microscopyWEHZ4 (best 0.88)
8Q1UInward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially…electron microscopyWEHZ3 (best 0.86)
8Q1YOutward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially…electron microscopyWEHZ4 (best 0.86)
8Q25Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially…electron microscopyWEHZ3 (best 0.86)
8Q45Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG.electron microscopyWEHZ3 (best 0.89)
8Q46Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyWEHZ4 (best 0.90)
8Q47Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.electron microscopyWEHZ4 (best 0.90)
8Q48Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.electron microscopyWEHZ3 (best 0.86)
8Q49Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyWEHZ3 (best 0.90)
8Q4AOutward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.electron microscopyWEHZ3 (best 0.86)
Q02366AlphaFold monomer V2.0 prediction for NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6…predictedA—1 (best 0.73)

Ligands

  • EHZ · ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate · in 39 records

Experiment against prediction

Elsewhere

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.