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Atomistry » Bromine » PDB 5i74-5l3j » 5ih6 » |
Bromine in PDB 5ih6: Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A DerivativeEnzymatic activity of Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A Derivative
All present enzymatic activity of Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A Derivative:
2.7.11.1; 2.7.11.26; Protein crystallography data
The structure of Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A Derivative, PDB code: 5ih6
was solved by
A.Ursu,
D.J.Illich,
Y.Takemoto,
A.T.Porfetye,
M.Zhang,
A.Brockmeyer,
P.Janning,
N.Watanabe,
H.Osada,
I.R.Vetter,
S.Ziegler,
H.R.Schoeler,
H.Waldmann,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5ih6:
The structure of Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A Derivative also contains other interesting chemical elements:
Bromine Binding Sites:
The binding sites of Bromine atom in the Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A Derivative
(pdb code 5ih6). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A Derivative, PDB code: 5ih6: Bromine binding site 1 out of 1 in 5ih6Go back to Bromine Binding Sites List in 5ih6
Bromine binding site 1 out
of 1 in the Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A Derivative
Mono view Stereo pair view
Reference:
A.Ursu,
D.J.Illich,
Y.Takemoto,
A.T.Porfetye,
M.Zhang,
A.Brockmeyer,
P.Janning,
N.Watanabe,
H.Osada,
I.R.Vetter,
S.Ziegler,
H.R.Scholer,
H.Waldmann.
Epiblastin A Induces Reprogramming of Epiblast Stem Cells Into Embryonic Stem Cells By Inhibition of Casein Kinase 1. Cell Chem Biol V. 23 494 2016.
Page generated: Thu Jul 11 00:03:52 2024
ISSN: ESSN 2451-9456 PubMed: 27049670 DOI: 10.1016/J.CHEMBIOL.2016.02.015 |
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