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Atomistry » Potassium » PDB 4eei-4gx0 » 4ged | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 4eei-4gx0 » 4ged » |
Potassium in PDB 4ged: Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C ComplexEnzymatic activity of Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex
All present enzymatic activity of Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex:
1.11.1.11; Protein crystallography data
The structure of Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex, PDB code: 4ged
was solved by
V.S.Jasion,
T.Doukov,
S.H.Pineda,
H.Li,
T.L.Poulos,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4ged:
The structure of Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex
(pdb code 4ged). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex, PDB code: 4ged: Potassium binding site 1 out of 1 in 4gedGo back to![]() ![]()
Potassium binding site 1 out
of 1 in the Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex
![]() Mono view ![]() Stereo pair view
Reference:
V.S.Jasion,
T.Doukov,
S.H.Pineda,
H.Li,
T.L.Poulos.
Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex. Proc.Natl.Acad.Sci.Usa V. 109 18390 2012.
Page generated: Mon Aug 12 10:49:24 2024
ISSN: ISSN 0027-8424 PubMed: 23100535 DOI: 10.1073/PNAS.1213295109 |
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