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Atomistry » Magnesium » PDB 1l3r-1lny » 1l4y » |
Magnesium in PDB 1l4y: Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp at 2.0 Angstrom ResolutionEnzymatic activity of Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp at 2.0 Angstrom Resolution
All present enzymatic activity of Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp at 2.0 Angstrom Resolution:
2.7.1.71; Protein crystallography data
The structure of Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp at 2.0 Angstrom Resolution, PDB code: 1l4y
was solved by
Y.Gu,
L.Reshetnikova,
Y.Li,
Y.Wu,
H.Yan,
S.Singh,
X.Ji,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1l4y:
The structure of Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp at 2.0 Angstrom Resolution also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp at 2.0 Angstrom Resolution
(pdb code 1l4y). 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 Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp at 2.0 Angstrom Resolution, PDB code: 1l4y: Magnesium binding site 1 out of 1 in 1l4yGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp at 2.0 Angstrom Resolution
![]() Mono view ![]() Stereo pair view
Reference:
Y.Gu,
L.Reshetnikova,
Y.Li,
Y.Wu,
H.Yan,
S.Singh,
X.Ji.
Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis Reveals the Dynamic Role of the Lid Domain in Catalysis. J.Mol.Biol. V. 319 779 2002.
Page generated: Tue Aug 13 08:26:23 2024
ISSN: ISSN 0022-2836 PubMed: 12054870 DOI: 10.1016/S0022-2836(02)00339-X |
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