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Atomistry » Sodium » PDB 5v0d-5vb7 » 5v4h » |
Sodium in PDB 5v4h: Ruthenium(II)(Cymene)(Chlorido)2-Lysozyme Adduct Formed When Ruthenium(II)(Cymene)(Bromido)2 Underwent Ligand Exchange, Resulting in One Binding SiteEnzymatic activity of Ruthenium(II)(Cymene)(Chlorido)2-Lysozyme Adduct Formed When Ruthenium(II)(Cymene)(Bromido)2 Underwent Ligand Exchange, Resulting in One Binding Site
All present enzymatic activity of Ruthenium(II)(Cymene)(Chlorido)2-Lysozyme Adduct Formed When Ruthenium(II)(Cymene)(Bromido)2 Underwent Ligand Exchange, Resulting in One Binding Site:
3.2.1.17; Protein crystallography data
The structure of Ruthenium(II)(Cymene)(Chlorido)2-Lysozyme Adduct Formed When Ruthenium(II)(Cymene)(Bromido)2 Underwent Ligand Exchange, Resulting in One Binding Site, PDB code: 5v4h
was solved by
M.P.Sullivan,
C.G.Hartinger,
D.C.Goldstone,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5v4h:
The structure of Ruthenium(II)(Cymene)(Chlorido)2-Lysozyme Adduct Formed When Ruthenium(II)(Cymene)(Bromido)2 Underwent Ligand Exchange, Resulting in One Binding Site also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Ruthenium(II)(Cymene)(Chlorido)2-Lysozyme Adduct Formed When Ruthenium(II)(Cymene)(Bromido)2 Underwent Ligand Exchange, Resulting in One Binding Site
(pdb code 5v4h). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Ruthenium(II)(Cymene)(Chlorido)2-Lysozyme Adduct Formed When Ruthenium(II)(Cymene)(Bromido)2 Underwent Ligand Exchange, Resulting in One Binding Site, PDB code: 5v4h: Sodium binding site 1 out of 1 in 5v4hGo back to Sodium Binding Sites List in 5v4h
Sodium binding site 1 out
of 1 in the Ruthenium(II)(Cymene)(Chlorido)2-Lysozyme Adduct Formed When Ruthenium(II)(Cymene)(Bromido)2 Underwent Ligand Exchange, Resulting in One Binding Site
Mono view Stereo pair view
Reference:
M.P.Sullivan,
M.Groessl,
S.M.Meier,
R.L.Kingston,
D.C.Goldstone,
C.G.Hartinger.
The Metalation of Hen Egg White Lysozyme Impacts Protein Stability As Shown By Ion Mobility Mass Spectrometry, Differential Scanning Calorimetry, and X-Ray Crystallography. Chem. Commun. (Camb.) V. 53 4246 2017.
Page generated: Tue Dec 15 11:44:09 2020
ISSN: ESSN 1364-548X PubMed: 28361137 DOI: 10.1039/C6CC10150J |
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