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Bromine in PDB 5ih6: Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A Derivative

Enzymatic 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:

Resolution Low / High (Å) 37.80 / 2.30
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 65.720, 65.720, 151.720, 90.00, 90.00, 120.00
R / Rfree (%) 23.3 / 26

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:

Zinc (Zn) 1 atom

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 5ih6

Go 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

A full contact list of Bromine with other atoms in the Br binding site number 1 of Human Casein Kinase 1 Isoform Delta (Kinase Domain) in Complex with Epiblastin A Derivative within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br305

b:94.2
occ:1.00
 BR A:AUG305 0.0 94.2 1.0
C15 A:AUG305 2.0 0.3 1.0
C16 A:AUG305 2.9 96.2 1.0
C14 A:AUG305 3.1 0.8 1.0
CG A:MET82 3.2 96.2 1.0
CE A:MET80 3.2 92.7 1.0
O A:MET80 3.7 73.6 1.0
CB A:LYS38 3.8 80.0 1.0
SD A:MET82 3.9 94.7 1.0
O A:ALA36 3.9 78.6 1.0
N A:LYS38 4.0 69.1 1.0
CG A:MET80 4.1 89.1 1.0
C11 A:AUG305 4.2 85.4 1.0
CB A:MET82 4.3 84.8 1.0
N A:MET82 4.3 77.2 1.0
C A:ALA36 4.4 72.8 1.0
C A:ILE37 4.4 71.6 1.0
C13 A:AUG305 4.4 0.3 1.0
C A:MET80 4.4 73.2 1.0
SD A:MET80 4.4 0.8 1.0
CB A:MET80 4.5 76.9 1.0
CA A:LYS38 4.5 77.6 1.0
N A:ILE37 4.6 78.6 1.0
CA A:ILE37 4.6 78.2 1.0
CG A:LYS38 4.7 94.2 1.0
CG2 A:ILE23 4.7 75.2 1.0
CB A:ALA36 4.8 73.3 1.0
CD1 A:ILE23 4.8 87.9 1.0
C12 A:AUG305 4.8 94.7 1.0
CD A:LYS38 4.8 0.6 1.0
C A:VAL81 4.9 73.3 1.0
CA A:MET82 4.9 76.3 1.0

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.
ISSN: ESSN 2451-9456
PubMed: 27049670
DOI: 10.1016/J.CHEMBIOL.2016.02.015
Page generated: Thu Jul 11 00:03:52 2024

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