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Atomistry » Magnesium » PDB 5fux-5gg7 » 5fux | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 5fux-5gg7 » 5fux » |
Magnesium in PDB 5fux: Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with DtmpEnzymatic activity of Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp
All present enzymatic activity of Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp:
2.7.1.21; Protein crystallography data
The structure of Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp, PDB code: 5fux
was solved by
J.Timm,
M.Valente,
V.Castillo-Acosta,
T.Balzarini,
J.E.Nettleship,
H.Rada,
K.S.Wilson,
D.Gonzalez-Pacanowska,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5fux:
The structure of Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp
(pdb code 5fux). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp, PDB code: 5fux: Magnesium binding site 1 out of 1 in 5fuxGo back to Magnesium Binding Sites List in 5fux
Magnesium binding site 1 out
of 1 in the Catalytic Domain of Thymidine Kinase From Trypanosoma Brucei with Dtmp
Mono view Stereo pair view
Reference:
M.Valente,
J.Timm,
V.M.Castillo-Acosta,
L.M.Ruiz-Perez,
T.Balzarini,
J.E.Nettleship,
L.E.Bird,
H.Rada,
K.S.Wilson,
D.Gonzalez-Pacanowska.
Cell Cycle Regulation and Novel Structural Features of Thymidine Kinase, An Essential Enzyme in Trypanosoma Brucei. Mol.Microbiol. V. 102 365 2016.
Page generated: Sun Sep 29 04:32:29 2024
ISSN: ISSN 0950-382X PubMed: 27426054 DOI: 10.1111/MMI.13467 |
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