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Atomistry » Chlorine » PDB 3bpr-3c4c » 3c13 » |
Chlorine in PDB 3c13: Low pH-Value Crystal Structure of Emodin in Complex with the Catalytic Subunit of Protein Kinase CK2Enzymatic activity of Low pH-Value Crystal Structure of Emodin in Complex with the Catalytic Subunit of Protein Kinase CK2
All present enzymatic activity of Low pH-Value Crystal Structure of Emodin in Complex with the Catalytic Subunit of Protein Kinase CK2:
2.7.11.1; Protein crystallography data
The structure of Low pH-Value Crystal Structure of Emodin in Complex with the Catalytic Subunit of Protein Kinase CK2, PDB code: 3c13
was solved by
K.Niefind,
J.Raaf,
O.-G.Issinger,
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 Low pH-Value Crystal Structure of Emodin in Complex with the Catalytic Subunit of Protein Kinase CK2
(pdb code 3c13). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Low pH-Value Crystal Structure of Emodin in Complex with the Catalytic Subunit of Protein Kinase CK2, PDB code: 3c13: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3c13Go back to Chlorine Binding Sites List in 3c13
Chlorine binding site 1 out
of 2 in the Low pH-Value Crystal Structure of Emodin in Complex with the Catalytic Subunit of Protein Kinase CK2
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 3c13Go back to Chlorine Binding Sites List in 3c13
Chlorine binding site 2 out
of 2 in the Low pH-Value Crystal Structure of Emodin in Complex with the Catalytic Subunit of Protein Kinase CK2
Mono view Stereo pair view
Reference:
J.Raaf,
K.Klopffleisch,
O.-G.Issinger,
K.Niefind.
The Catalytic Subunit of Human Protein Kinase CK2 Structurally Deviates From Its Maize Homologue in Complex with the Nucleotide Competitive Inhibitor Emodin J.Mol.Biol. V. 377 1 2008.
Page generated: Sat Dec 12 09:33:59 2020
ISSN: ISSN 0022-2836 PubMed: 18242640 DOI: 10.1016/J.JMB.2008.01.008 |
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