Fluorine in PDB 6f1w: Crystal Structure of Human Casein Kinase I Delta in Complex with Compound 31A

All present enzymatic activity of Crystal Structure of Human Casein Kinase I Delta in Complex with Compound 31A:
2.7.11.1; 2.7.11.26;

The structure of Crystal Structure of Human Casein Kinase I Delta in Complex with Compound 31A, PDB code: 6f1w was solved by C.Pichlo, E.Brunstein, U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.81 / 1.86
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	51.549, 105.872, 71.687, 90.00, 108.93, 90.00
R / Rfree (%)	18.1 / 20.6

The binding sites of Fluorine atom in the Crystal Structure of Human Casein Kinase I Delta in Complex with Compound 31A (pdb code 6f1w). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Human Casein Kinase I Delta in Complex with Compound 31A, PDB code: 6f1w:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Human Casein Kinase I Delta in Complex with Compound 31A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human Casein Kinase I Delta in Complex with Compound 31A within 5.0Å range: probe atom residue distance (Å) B Occ A:F308 b:38.8 occ:1.00 F32 A:CG5308 0.0 38.8 1.0 C31 A:CG5308 1.3 36.7 1.0 C30 A:CG5308 2.3 36.3 1.0 C33 A:CG5308 2.3 33.1 1.0 H301 A:CG5308 2.5 43.5 1.0 H331 A:CG5308 2.6 39.7 1.0 HG2 A:MET80 2.7 54.3 1.0 HB2 A:MET82 2.7 34.5 1.0 HB3 A:MET80 2.9 47.2 1.0 HE2 A:MET80 3.1 52.9 1.0 HE3 A:MET80 3.2 52.9 1.0 HB3 A:MET82 3.3 34.5 1.0 O A:MET80 3.3 33.2 1.0 HE3 A:MET82 3.3 36.0 1.0 CB A:MET82 3.4 28.8 1.0 HB3 A:LYS38 3.4 48.7 1.0 CG A:MET80 3.5 45.3 1.0 C29 A:CG5308 3.5 36.0 1.0 C34 A:CG5308 3.5 35.2 1.0 CE A:MET80 3.5 44.1 1.0 C A:MET80 3.6 35.5 1.0 CB A:MET80 3.6 39.4 1.0 HB2 A:LYS38 3.7 48.7 1.0 H A:LYS38 3.7 44.2 1.0 H A:MET82 3.7 33.2 1.0 N A:MET82 3.7 27.7 1.0 HD12 A:ILE68 3.9 43.7 1.0 C A:VAL81 4.0 31.6 1.0 HA A:VAL81 4.0 38.5 1.0 CB A:LYS38 4.0 40.6 1.0 N A:VAL81 4.0 34.8 1.0 C28 A:CG5308 4.0 36.4 1.0 CA A:MET82 4.2 29.9 1.0 O A:ALA36 4.2 29.4 1.0 CA A:MET80 4.2 36.9 1.0 CE A:MET82 4.2 30.1 1.0 CA A:VAL81 4.2 32.1 1.0 HG3 A:MET80 4.2 54.3 1.0 N A:LYS38 4.3 36.9 1.0 SD A:MET80 4.3 48.1 1.0 HB2 A:MET80 4.4 47.2 1.0 HE1 A:MET80 4.4 52.9 1.0 H291 A:CG5308 4.4 43.2 1.0 H341 A:CG5308 4.4 42.2 1.0 HA A:ILE37 4.5 42.1 1.0 H A:VAL81 4.5 41.8 1.0 HA A:MET82 4.5 35.9 1.0 O A:VAL81 4.6 33.4 1.0 HE1 A:MET82 4.6 36.0 1.0 CG A:MET82 4.6 29.4 1.0 CD1 A:ILE68 4.6 36.4 1.0 HD3 A:LYS38 4.7 55.8 1.0 HD11 A:ILE68 4.7 43.7 1.0 HD13 A:ILE68 4.7 43.7 1.0 SD A:MET82 4.8 29.4 1.0 HD2 A:LYS38 4.8 55.8 1.0 CA A:LYS38 4.8 39.2 1.0 HE2 A:MET82 4.8 36.0 1.0 HA A:MET80 4.9 44.3 1.0 H A:MET80 4.9 44.2 1.0 HG3 A:MET82 5.0 35.2 1.0 HG23 A:ILE68 5.0 41.5 1.0 C A:ALA36 5.0 31.0 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Human Casein Kinase I Delta in Complex with Compound 31A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Human Casein Kinase I Delta in Complex with Compound 31A within 5.0Å range: probe atom residue distance (Å) B Occ B:F309 b:33.1 occ:1.00 F32 B:CG5309 0.0 33.1 1.0 C31 B:CG5309 1.3 30.8 1.0 C33 B:CG5309 2.3 28.6 1.0 C30 B:CG5309 2.3 31.6 1.0 H301 B:CG5309 2.5 37.9 1.0 H331 B:CG5309 2.6 34.3 1.0 HG2 B:MET80 2.8 48.3 1.0 HB2 B:MET82 2.8 29.1 1.0 HB3 B:MET80 2.9 40.5 1.0 HE3 B:MET80 3.0 45.9 1.0 HE3 B:MET82 3.2 28.8 1.0 HE2 B:MET80 3.2 45.9 1.0 HB3 B:MET82 3.3 29.1 1.0 O B:MET80 3.3 29.5 1.0 HB3 B:LYS38 3.4 45.4 1.0 CB B:MET82 3.4 24.3 1.0 C34 B:CG5309 3.5 29.6 1.0 C29 B:CG5309 3.5 29.2 1.0 CE B:MET80 3.5 38.2 1.0 CG B:MET80 3.5 40.3 1.0 C B:MET80 3.6 30.0 1.0 CB B:MET80 3.6 33.8 1.0 HB2 B:LYS38 3.6 45.4 1.0 H B:MET82 3.8 27.4 1.0 HD12 B:ILE68 3.8 45.0 1.0 N B:MET82 3.8 22.9 1.0 H B:LYS38 3.8 34.8 1.0 CB B:LYS38 4.0 37.9 1.0 C28 B:CG5309 4.0 30.0 1.0 HA B:VAL81 4.0 35.0 1.0 C B:VAL81 4.0 25.9 1.0 N B:VAL81 4.0 31.0 1.0 CE B:MET82 4.1 24.1 1.0 CA B:MET82 4.2 25.1 1.0 CA B:MET80 4.2 33.2 1.0 O B:ALA36 4.2 27.3 1.0 CA B:VAL81 4.3 29.2 1.0 HG3 B:MET80 4.3 48.3 1.0 SD B:MET80 4.3 42.9 1.0 HE1 B:MET80 4.4 45.9 1.0 N B:LYS38 4.4 29.0 1.0 H341 B:CG5309 4.4 35.5 1.0 H291 B:CG5309 4.4 35.0 1.0 HB2 B:MET80 4.4 40.5 1.0 CD1 B:ILE68 4.5 37.6 1.0 HD11 B:ILE68 4.5 45.0 1.0 HD3 B:LYS38 4.5 55.9 1.0 HE1 B:MET82 4.5 28.8 1.0 H B:VAL81 4.6 37.2 1.0 O B:VAL81 4.6 27.5 1.0 HA B:ILE37 4.6 30.5 1.0 HA B:MET82 4.6 30.1 1.0 HD2 B:LYS38 4.6 55.9 1.0 CG B:MET82 4.6 26.8 1.0 HD13 B:ILE68 4.6 45.0 1.0 SD B:MET82 4.7 26.0 1.0 HE2 B:MET82 4.7 28.8 1.0 CA B:LYS38 4.8 34.4 1.0 H B:MET80 4.9 40.2 1.0 HA B:MET80 4.9 39.8 1.0 CD B:LYS38 4.9 46.6 1.0 HG23 B:ILE68 5.0 40.0 1.0 HG3 B:MET82 5.0 32.1 1.0

A.Luxenburger, D.Schmidt, C.Ianes, C.Pichlo, M.Kruger, T.Von Drathen, E.Brunstein, G.J.Gainsford, U.Baumann, U.Knippschild, C.Peifer. Design, Synthesis and Biological Evaluation of Isoxazole-Based CK1 Inhibitors Modified with Chiral Pyrrolidine Scaffolds. Molecules V. 24 2019.
ISSN: ESSN 1420-3049
PubMed: 30832206
DOI: 10.3390/MOLECULES24050873