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Atomistry » Magnesium » PDB 5skf-5t2v » 5svt | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 5skf-5t2v » 5svt » |
Magnesium in PDB 5svt: Anomalous Cs+ Signal Reveals the Site of Na+ Ion Entry to the Channel Pore of the Human P2X3 Ion Channel Through the Extracellular FenestrationsProtein crystallography data
The structure of Anomalous Cs+ Signal Reveals the Site of Na+ Ion Entry to the Channel Pore of the Human P2X3 Ion Channel Through the Extracellular Fenestrations, PDB code: 5svt
was solved by
S.E.Mansoor,
W.Lu,
W.Oosterheert,
M.Shekhar,
E.Tajkhorshid,
E.Gouaux,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5svt:
The structure of Anomalous Cs+ Signal Reveals the Site of Na+ Ion Entry to the Channel Pore of the Human P2X3 Ion Channel Through the Extracellular Fenestrations also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Anomalous Cs+ Signal Reveals the Site of Na+ Ion Entry to the Channel Pore of the Human P2X3 Ion Channel Through the Extracellular Fenestrations
(pdb code 5svt). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Anomalous Cs+ Signal Reveals the Site of Na+ Ion Entry to the Channel Pore of the Human P2X3 Ion Channel Through the Extracellular Fenestrations, PDB code: 5svt: Magnesium binding site 1 out of 1 in 5svtGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Anomalous Cs+ Signal Reveals the Site of Na+ Ion Entry to the Channel Pore of the Human P2X3 Ion Channel Through the Extracellular Fenestrations
![]() Mono view ![]() Stereo pair view
Reference:
S.E.Mansoor,
W.Lu,
W.Oosterheert,
M.Shekhar,
E.Tajkhorshid,
E.Gouaux.
X-Ray Structures Define Human P2X3 Receptor Gating Cycle and Antagonist Action. Nature V. 538 66 2016.
Page generated: Mon Sep 30 04:41:04 2024
ISSN: ESSN 1476-4687 PubMed: 27626375 DOI: 10.1038/NATURE19367 |
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