Fluorine in PDB 6nzm: Brutons Tyrosine Kinase in Complex with Compound 50.

All present enzymatic activity of Brutons Tyrosine Kinase in Complex with Compound 50.:
2.7.10.2;

The structure of Brutons Tyrosine Kinase in Complex with Compound 50., PDB code: 6nzm was solved by D.J.Marcotte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.31 / 1.72
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.297, 71.709, 104.410, 90.00, 89.95, 90.00
R / Rfree (%)	17.6 / 24.8

The binding sites of Fluorine atom in the Brutons Tyrosine Kinase in Complex with Compound 50. (pdb code 6nzm). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Brutons Tyrosine Kinase in Complex with Compound 50., PDB code: 6nzm:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Brutons Tyrosine Kinase in Complex with Compound 50.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Brutons Tyrosine Kinase in Complex with Compound 50. within 5.0Å range: probe atom residue distance (Å) B Occ A:F701 b:30.6 occ:1.00 F1 A:L9S701 0.0 30.6 1.0 C13 A:L9S701 1.3 32.2 1.0 C14 A:L9S701 2.3 27.0 1.0 C12 A:L9S701 2.4 26.8 1.0 N3 A:L9S701 2.8 23.5 1.0 O2 A:L9S701 2.8 30.5 1.0 C11 A:L9S701 3.0 26.9 1.0 CD1 A:ILE432 3.1 38.6 1.0 C15 A:L9S701 3.5 30.4 1.0 CD A:LYS430 3.6 42.2 1.0 C17 A:L9S701 3.6 27.6 1.0 CG A:LYS430 3.9 40.8 1.0 C16 A:L9S701 4.0 31.5 1.0 N2 A:L9S701 4.1 26.5 1.0 CB A:PHE413 4.2 29.6 1.0 O A:PHE413 4.4 47.3 1.0 CD1 A:LEU542 4.5 34.5 1.0 CG1 A:ILE432 4.6 35.9 1.0 C A:PHE413 4.6 42.7 1.0 CD1 A:ILE472 4.8 32.1 1.0 CE A:LYS430 4.9 51.3 1.0 N4 A:L9S701 4.9 24.5 1.0 OD1 A:ASP539 4.9 30.6 1.0 O A:HOH833 5.0 39.7 1.0

Fluorine binding site 2 out of 2 in the Brutons Tyrosine Kinase in Complex with Compound 50.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Brutons Tyrosine Kinase in Complex with Compound 50. within 5.0Å range: probe atom residue distance (Å) B Occ D:F701 b:35.6 occ:1.00 F1 D:L9S701 0.0 35.6 1.0 C13 D:L9S701 1.4 31.7 1.0 C12 D:L9S701 2.4 26.9 1.0 C14 D:L9S701 2.4 31.8 1.0 N3 D:L9S701 2.8 28.0 1.0 CD1 D:ILE432 3.1 33.6 1.0 C11 D:L9S701 3.1 27.8 1.0 O2 D:L9S701 3.2 29.0 1.0 CD D:LYS430 3.5 38.7 1.0 C17 D:L9S701 3.6 25.7 1.0 C15 D:L9S701 3.7 28.6 1.0 CG D:LYS430 4.0 36.9 1.0 CB D:PHE413 4.1 39.5 1.0 C16 D:L9S701 4.2 23.4 1.0 O D:PHE413 4.2 32.2 1.0 N2 D:L9S701 4.2 29.2 1.0 C D:PHE413 4.4 38.9 1.0 CD1 D:LEU542 4.5 37.2 1.0 CG1 D:ILE432 4.6 32.6 1.0 N D:GLY414 4.7 40.5 1.0 N4 D:L9S701 4.8 25.6 1.0 CE D:LYS430 4.8 38.1 1.0 NZ D:LYS430 4.9 41.9 1.0 CA D:GLY414 4.9 42.6 1.0 CA D:PHE413 5.0 40.8 1.0 CD1 D:ILE472 5.0 29.2 1.0

B.T.Hopkins, E.Bame, N.Bell, T.Bohnert, J.K.Bowden-Verhoek, M.Bui, M.T.Cancilla, P.Conlon, P.Cullen, D.A.Erlanson, J.Fan, T.Fuchs-Knotts, S.Hansen, S.Heumann, T.J.Jenkins, D.Marcotte, B.Mcdowell, E.Mertsching, E.Negrou, K.L.Otipoby, U.Poreci, M.J.Romanowski, D.Scott, L.Silvian, W.Yang, M.Zhong. Optimization of Novel Reversible Bruton'S Tyrosine Kinase Inhibitors Identified Using Tethering-Fragment-Based Screens. Bioorg.Med.Chem. V. 27 2905 2019.
ISSN: ESSN 1464-3391
PubMed: 31138459
DOI: 10.1016/J.BMC.2019.05.021