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Atomistry » Iron » PDB 5kja-5ktp » 5kqh | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Iron » PDB 5kja-5ktp » 5kqh » |
Iron in PDB 5kqh: Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. PseudomalleiEnzymatic activity of Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei
All present enzymatic activity of Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei:
1.11.1.21; Protein crystallography data
The structure of Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kqh
was solved by
P.C.Loewen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5kqh:
The structure of Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei
(pdb code 5kqh). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kqh: Jump to Iron binding site number: 1; 2; Iron binding site 1 out of 2 in 5kqhGo back to![]() ![]()
Iron binding site 1 out
of 2 in the Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei
![]() Mono view ![]() Stereo pair view
Iron binding site 2 out of 2 in 5kqhGo back to![]() ![]()
Iron binding site 2 out
of 2 in the Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei
![]() Mono view ![]() Stereo pair view
Reference:
M.Machuqueiro,
B.Victor,
J.Switala,
J.Villanueva,
C.Rovira,
I.Fita,
P.C.Loewen.
The Catalase Activity of Catalase-Peroxidases Is Modulated By Changes in the Pka of the Distal Histidine. Biochemistry V. 56 2271 2017.
Page generated: Tue Aug 6 03:35:41 2024
ISSN: ISSN 1520-4995 PubMed: 28409923 DOI: 10.1021/ACS.BIOCHEM.6B01276 |
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