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Atomistry » Magnesium » PDB 1nzz-1oev » 1o6y | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1nzz-1oev » 1o6y » |
Magnesium in PDB 1o6y: Catalytic Domain of Pknb Kinase From Mycobacterium TuberculosisEnzymatic activity of Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis
All present enzymatic activity of Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis:
2.7.11.1; Protein crystallography data
The structure of Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis, PDB code: 1o6y
was solved by
M.Ortiz-Lombardia,
F.Pompeo,
B.Boitel,
P.M.Alzari,
Tb Structural Genomicsconsortium (Tbsgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis
(pdb code 1o6y). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis, PDB code: 1o6y: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 1o6yGo back to Magnesium Binding Sites List in 1o6y
Magnesium binding site 1 out
of 2 in the Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 1o6yGo back to Magnesium Binding Sites List in 1o6y
Magnesium binding site 2 out
of 2 in the Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis
Mono view Stereo pair view
Reference:
M.Ortiz-Lombardia,
F.Pompeo,
B.Boitel,
P.M.Alzari.
Crystal Structure of the Catalytic Domain of the Pknb Serine/Threonine Kinase From Mycobacterium Tuberculosis J.Biol.Chem. V. 278 13094 2003.
Page generated: Mon Dec 14 06:34:22 2020
ISSN: ISSN 0021-9258 PubMed: 12551895 DOI: 10.1074/JBC.M300660200 |
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