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Atomistry » Ruthenium » PDB 5iu5-6bo1 » 5v4h » |
Ruthenium 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:
Ruthenium Binding Sites:
The binding sites of Ruthenium 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 Ruthenium atom.
In total only one binding site of Ruthenium 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: Ruthenium binding site 1 out of 1 in 5v4hGo back to![]() ![]()
Ruthenium 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: Thu Oct 10 13:03:21 2024
ISSN: ESSN 1364-548X PubMed: 28361137 DOI: 10.1039/C6CC10150J |
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