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Atomistry » Chlorine » PDB 3o6j-3ohg » 3ofm » |
Chlorine in PDB 3ofm: Structure of A Human CK2ALPHA Prime, the Paralog Isoform of the Catalytic Subunit of Protein Kinase CK2 From Homo SapiensEnzymatic activity of Structure of A Human CK2ALPHA Prime, the Paralog Isoform of the Catalytic Subunit of Protein Kinase CK2 From Homo Sapiens
All present enzymatic activity of Structure of A Human CK2ALPHA Prime, the Paralog Isoform of the Catalytic Subunit of Protein Kinase CK2 From Homo Sapiens:
2.7.11.1; Protein crystallography data
The structure of Structure of A Human CK2ALPHA Prime, the Paralog Isoform of the Catalytic Subunit of Protein Kinase CK2 From Homo Sapiens, PDB code: 3ofm
was solved by
N.Bischoff,
B.Olsen,
J.Raaf,
M.Bretner,
O.-G.Issinger,
K.Niefind,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3ofm:
The structure of Structure of A Human CK2ALPHA Prime, the Paralog Isoform of the Catalytic Subunit of Protein Kinase CK2 From Homo Sapiens also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structure of A Human CK2ALPHA Prime, the Paralog Isoform of the Catalytic Subunit of Protein Kinase CK2 From Homo Sapiens
(pdb code 3ofm). 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 Human CK2ALPHA Prime, the Paralog Isoform of the Catalytic Subunit of Protein Kinase CK2 From Homo Sapiens, PDB code: 3ofm: Chlorine binding site 1 out of 1 in 3ofmGo back to Chlorine Binding Sites List in 3ofm
Chlorine binding site 1 out
of 1 in the Structure of A Human CK2ALPHA Prime, the Paralog Isoform of the Catalytic Subunit of Protein Kinase CK2 From Homo Sapiens
Mono view Stereo pair view
Reference:
N.Bischoff,
B.Olsen,
J.Raaf,
M.Bretner,
O.G.Issinger,
K.Niefind.
Structural Basis of the Reduced Affinity Between the Protein Kinase CK2 Subunits CK2ALPHA Prime and CK2BETA J.Mol.Biol. V. 407 1 2011.
Page generated: Sun Jul 21 01:37:54 2024
ISSN: ISSN 0022-2836 PubMed: 21241709 DOI: 10.1016/J.JMB.2011.01.020 |
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