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Atomistry » Zinc » PDB 4xo3-4y87 » 4y0x | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4xo3-4y87 » 4y0x » |
Zinc in PDB 4y0x: Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with AdpEnzymatic activity of Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Adp
All present enzymatic activity of Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Adp:
2.7.11.1; Protein crystallography data
The structure of Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Adp, PDB code: 4y0x
was solved by
M.N.Lisa,
P.M.Alzari,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4y0x:
The structure of Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Adp also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Adp
(pdb code 4y0x). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Adp, PDB code: 4y0x: Zinc binding site 1 out of 1 in 4y0xGo back to Zinc Binding Sites List in 4y0x
Zinc binding site 1 out
of 1 in the Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Adp
Mono view Stereo pair view
Reference:
M.N.Lisa,
M.Gil,
G.Andre-Leroux,
N.Barilone,
R.Duran,
R.M.Biondi,
P.M.Alzari.
Molecular Basis of the Activity and the Regulation of the Eukaryotic-Like S/T Protein Kinase Pkng From Mycobacterium Tuberculosis. Structure 2015.
Page generated: Sun Oct 27 10:54:47 2024
ISSN: ISSN 0969-2126 PubMed: 25960409 DOI: 10.1016/J.STR.2015.04.001 |
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