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Atomistry » Chlorine » PDB 3u69-3ue4 » 3u9c » |
Chlorine in PDB 3u9c: Structure of A C-Terminal Deletion Mutant of Human Protein Kinase CK2 Catalytic Subunit with the Atp-Competitive Inhibitor ResorufinEnzymatic activity of Structure of A C-Terminal Deletion Mutant of Human Protein Kinase CK2 Catalytic Subunit with the Atp-Competitive Inhibitor Resorufin
All present enzymatic activity of Structure of A C-Terminal Deletion Mutant of Human Protein Kinase CK2 Catalytic Subunit with the Atp-Competitive Inhibitor Resorufin:
2.7.11.1; Protein crystallography data
The structure of Structure of A C-Terminal Deletion Mutant of Human Protein Kinase CK2 Catalytic Subunit with the Atp-Competitive Inhibitor Resorufin, PDB code: 3u9c
was solved by
K.Klopffleisch,
O.-G.Issinger,
K.Niefind,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structure of A C-Terminal Deletion Mutant of Human Protein Kinase CK2 Catalytic Subunit with the Atp-Competitive Inhibitor Resorufin
(pdb code 3u9c). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of A C-Terminal Deletion Mutant of Human Protein Kinase CK2 Catalytic Subunit with the Atp-Competitive Inhibitor Resorufin, PDB code: 3u9c: Chlorine binding site 1 out of 1 in 3u9cGo back to Chlorine Binding Sites List in 3u9c
Chlorine binding site 1 out
of 1 in the Structure of A C-Terminal Deletion Mutant of Human Protein Kinase CK2 Catalytic Subunit with the Atp-Competitive Inhibitor Resorufin
Mono view Stereo pair view
Reference:
K.Klopffleisch,
O.G.Issinger,
K.Niefind.
Low-Density Crystal Packing of Human Protein Kinase CK2 Catalytic Subunit in Complex with Resorufin or Other Ligands: A Tool to Study the Unique Hinge-Region Plasticity of the Enzyme Without Packing Bias. Acta Crystallogr.,Sect.D V. 68 883 2012.
Page generated: Sat Dec 12 10:14:20 2020
ISSN: ISSN 0907-4449 PubMed: 22868753 DOI: 10.1107/S0907444912016587 |
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