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Magnesium in PDB 8eig: The Complex of Phosphorylated Human Delta F508 Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) with Elexacaftor (Vx-445) and Atp/MgEnzymatic activity of The Complex of Phosphorylated Human Delta F508 Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) with Elexacaftor (Vx-445) and Atp/Mg
All present enzymatic activity of The Complex of Phosphorylated Human Delta F508 Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) with Elexacaftor (Vx-445) and Atp/Mg:
5.6.1.6; Other elements in 8eig:
The structure of The Complex of Phosphorylated Human Delta F508 Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) with Elexacaftor (Vx-445) and Atp/Mg also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The Complex of Phosphorylated Human Delta F508 Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) with Elexacaftor (Vx-445) and Atp/Mg
(pdb code 8eig). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Complex of Phosphorylated Human Delta F508 Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) with Elexacaftor (Vx-445) and Atp/Mg, PDB code: 8eig: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 8eigGo back to Magnesium Binding Sites List in 8eig
Magnesium binding site 1 out
of 2 in the The Complex of Phosphorylated Human Delta F508 Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) with Elexacaftor (Vx-445) and Atp/Mg
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 8eigGo back to Magnesium Binding Sites List in 8eig
Magnesium binding site 2 out
of 2 in the The Complex of Phosphorylated Human Delta F508 Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) with Elexacaftor (Vx-445) and Atp/Mg
Mono view Stereo pair view
Reference:
K.Fiedorczuk,
J.Chen.
Molecular Structures Reveal Synergistic Rescue of Delta 508 Cftr By Trikafta Modulators. Science V. 378 284 2022.
Page generated: Fri Apr 7 09:27:13 2023
ISSN: ESSN 1095-9203 PubMed: 36264792 DOI: 10.1126/SCIENCE.ADE2216 |
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