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Atomistry » Sodium » PDB 4qon-4r3n » 4qor | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 4qon-4r3n » 4qor » |
Sodium in PDB 4qor: Structure of Bacillus Pumilus Catalase with Chlorophenol Bound.Enzymatic activity of Structure of Bacillus Pumilus Catalase with Chlorophenol Bound.
All present enzymatic activity of Structure of Bacillus Pumilus Catalase with Chlorophenol Bound.:
1.11.1.6; Protein crystallography data
The structure of Structure of Bacillus Pumilus Catalase with Chlorophenol Bound., PDB code: 4qor
was solved by
P.C.Loewen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4qor:
The structure of Structure of Bacillus Pumilus Catalase with Chlorophenol Bound. also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of Bacillus Pumilus Catalase with Chlorophenol Bound.
(pdb code 4qor). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structure of Bacillus Pumilus Catalase with Chlorophenol Bound., PDB code: 4qor: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 4qorGo back to![]() ![]()
Sodium binding site 1 out
of 2 in the Structure of Bacillus Pumilus Catalase with Chlorophenol Bound.
![]() Mono view ![]() Stereo pair view
Sodium binding site 2 out of 2 in 4qorGo back to![]() ![]()
Sodium binding site 2 out
of 2 in the Structure of Bacillus Pumilus Catalase with Chlorophenol Bound.
![]() Mono view ![]() Stereo pair view
Reference:
P.C.Loewen,
J.Villanueva,
J.Switala,
L.J.Donald,
A.Ivancich.
Unprecedented Access of Phenolic Substrates to the Heme Active Site of A Catalase: Substrate Binding and Peroxidase-Like Reactivity of Bacillus Pumilus Catalase Monitored By X-Ray Crystallography and Epr Spectroscopy. Proteins 2015.
Page generated: Mon Oct 7 18:05:21 2024
ISSN: ESSN 1097-0134 PubMed: 25663126 DOI: 10.1002/PROT.24777 |
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