Chlorine in PDB 6s11: Crystal Structure of DYRK1A with Small Molecule Inhibitor

All present enzymatic activity of Crystal Structure of DYRK1A with Small Molecule Inhibitor:
2.7.12.1;

The structure of Crystal Structure of DYRK1A with Small Molecule Inhibitor, PDB code: 6s11 was solved by F.J.Sorrell, S.H.Henderson, C.Redondo, N.A.Burgess-Brown, F.Von Delft, C.H.Arrowsmith, C.Bountra, A.M.Edwards, J.M.Elkins, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	84.31 / 2.45
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	168.615, 168.615, 62.154, 90.00, 90.00, 120.00
R / Rfree (%)	17.1 / 21

The structure of Crystal Structure of DYRK1A with Small Molecule Inhibitor also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Chlorine atom in the Crystal Structure of DYRK1A with Small Molecule Inhibitor (pdb code 6s11). 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 Crystal Structure of DYRK1A with Small Molecule Inhibitor, PDB code: 6s11:

Chlorine binding site 1 out of 1 in the Crystal Structure of DYRK1A with Small Molecule Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of DYRK1A with Small Molecule Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:25.7 occ:1.00 N A:HIS424 3.3 14.4 1.0 CB A:HIS424 3.5 14.2 1.0 O A:HOH776 3.5 19.8 1.0 NZ A:LYS453 3.6 23.8 1.0 O A:HOH818 3.8 51.0 1.0 CD A:LYS453 3.8 16.9 1.0 N A:LEU423 3.8 21.6 1.0 CA A:HIS424 4.0 17.4 1.0 CD A:LYS422 4.1 22.6 1.0 CE A:LYS453 4.1 18.5 1.0 CB A:LYS422 4.2 22.9 1.0 C A:LEU423 4.3 16.5 1.0 CA A:LEU423 4.4 18.3 1.0 C A:LYS422 4.4 22.1 1.0 CB A:LEU423 4.5 17.1 1.0 CA A:LYS422 4.5 20.6 1.0 CG A:LYS422 4.7 21.0 1.0 CG A:LYS453 4.7 16.8 1.0 CD1 A:LEU457 4.7 15.6 1.0 CG A:HIS424 4.7 15.0 1.0

F.J.Sorrell, S.H.Henderson, J.M.Elkins, S.Ward. Kinase Scaffold Repurposing in the Public Domain To Be Published.