Chlorine in PDB 8siw: Structure of Compound 5 Bound to the CHK1 10-Point Mutant

All present enzymatic activity of Structure of Compound 5 Bound to the CHK1 10-Point Mutant:
2.7.11.1;

The structure of Structure of Compound 5 Bound to the CHK1 10-Point Mutant, PDB code: 8siw was solved by R.L.Palte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	108.17 / 1.88
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.998, 66.121, 110.295, 90, 101.27, 90
R / Rfree (%)	21.9 / 25.8

The binding sites of Chlorine atom in the Structure of Compound 5 Bound to the CHK1 10-Point Mutant (pdb code 8siw). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Compound 5 Bound to the CHK1 10-Point Mutant, PDB code: 8siw:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Compound 5 Bound to the CHK1 10-Point Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Compound 5 Bound to the CHK1 10-Point Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:44.8 occ:1.00 CL A:ZXL301 0.0 44.8 1.0 C6 A:ZXL301 1.7 44.1 1.0 C5 A:ZXL301 2.7 44.3 1.0 C7 A:ZXL301 2.7 43.5 1.0 C9 A:ZXL301 3.1 42.5 1.0 C10 A:ZXL301 3.6 42.0 1.0 C8 A:ZXL301 4.0 43.8 1.0 C3 A:ZXL301 4.0 44.6 1.0 CG2 A:VAL23 4.0 71.2 1.0 O A:HOH503 4.1 30.2 1.0 SD A:MET84 4.1 66.4 1.0 N A:ASP148 4.1 26.9 1.0 CB A:ALA147 4.2 27.0 1.0 C13 A:ZXL301 4.5 41.9 1.0 CA A:ASP148 4.5 27.0 1.0 C2 A:ZXL301 4.5 44.4 1.0 C11 A:ZXL301 4.6 41.8 1.0 CB A:ASP148 4.6 28.7 1.0 CG1 A:VAL23 4.7 71.1 1.0 O A:HOH493 4.8 41.1 1.0 C A:ALA147 4.9 27.0 1.0 CB A:VAL23 5.0 70.8 1.0

Chlorine binding site 2 out of 2 in the Structure of Compound 5 Bound to the CHK1 10-Point Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Compound 5 Bound to the CHK1 10-Point Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:45.3 occ:1.00 CL B:ZXL301 0.0 45.3 1.0 C6 B:ZXL301 1.7 44.0 1.0 C5 B:ZXL301 2.7 44.0 1.0 C7 B:ZXL301 2.7 42.8 1.0 CE B:MET84 3.0 67.3 1.0 C9 B:ZXL301 3.1 41.6 1.0 C10 B:ZXL301 3.5 41.0 1.0 N B:ASP148 3.8 36.2 1.0 SD B:MET84 3.9 67.0 1.0 C8 B:ZXL301 4.0 43.0 1.0 C3 B:ZXL301 4.0 43.9 1.0 CA B:ASP148 4.1 37.1 1.0 CB B:ALA147 4.2 35.9 1.0 CB B:ASP148 4.2 40.0 1.0 CG2 B:VAL23 4.3 66.2 1.0 C13 B:ZXL301 4.5 41.0 1.0 C2 B:ZXL301 4.5 43.5 1.0 C11 B:ZXL301 4.5 40.6 1.0 C B:ALA147 4.7 36.1 1.0 O B:HOH455 4.7 25.1 1.0 CG1 B:VAL23 4.8 66.2 1.0 CA B:ALA147 4.9 35.9 1.0 CG B:ASP148 5.0 45.9 1.0

S.D.Kattar, A.Gulati, K.A.Margrey, M.H.Keylor, M.Ardolino, X.Yan, R.Johnson, R.L.Palte, S.E.Mcminn, L.Nogle, J.Su, D.Xiao, J.Piesvaux, S.Lee, L.G.Hegde, J.D.Woodhouse, R.Faltus, L.Y.Moy, T.Xiong, P.J.Ciaccio, K.Pearson, M.Patel, K.M.Otte, C.E.G.Leyns, M.E.Kennedy, D.J.Bennett, E.F.Dimauro, M.J.Fell, P.H.Fuller. Discovery of Mk-1468: A Potent, Kinome-Selective, Brain-Penetrant Amidoisoquinoline LRRK2 Inhibitor For the Potential Treatment of Parkinson'S Disease. J.Med.Chem. 2023.
ISSN: ISSN 0022-2623
PubMed: 37861679
DOI: 10.1021/ACS.JMEDCHEM.3C01486