Fluorine in PDB 7mck: Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18

All present enzymatic activity of Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18:
2.7.11.1;

The structure of Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18, PDB code: 7mck was solved by R.Palte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.94 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.98, 65.37, 54.07, 90, 102.32, 90
R / Rfree (%)	19.2 / 22.5

The binding sites of Fluorine atom in the Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18 (pdb code 7mck). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18, PDB code: 7mck:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:47.5 occ:1.00 F2 A:YXD301 0.0 47.5 1.0 C4 A:YXD301 1.3 46.5 1.0 F1 A:YXD301 2.1 47.7 1.0 F A:YXD301 2.1 47.1 1.0 C3 A:YXD301 2.4 43.1 1.0 N1 A:YXD301 2.6 43.4 1.0 O A:HOH508 2.7 44.7 1.0 O A:LEU15 3.5 49.8 1.0 C2 A:YXD301 3.7 41.1 1.0 O A:HOH482 3.9 39.3 1.0 C5 A:YXD301 4.0 45.7 1.0 N A:YXD301 4.1 35.4 1.0 C A:LEU15 4.3 50.8 1.0 CA A:GLY16 4.4 51.2 1.0 O A:HIS134 4.5 24.5 1.0 CD2 A:LEU137 4.6 28.6 1.0 N A:GLY16 4.7 50.0 1.0 C14 A:YXD301 4.8 43.1 1.0 C6 A:YXD301 4.9 46.8 1.0

Fluorine binding site 2 out of 3 in the Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:47.1 occ:1.00 F A:YXD301 0.0 47.1 1.0 C4 A:YXD301 1.3 46.5 1.0 F1 A:YXD301 2.1 47.7 1.0 F2 A:YXD301 2.1 47.5 1.0 C3 A:YXD301 2.4 43.1 1.0 N A:YXD301 2.9 35.4 1.0 C2 A:YXD301 3.0 41.1 1.0 N1 A:YXD301 3.3 43.4 1.0 O A:LEU15 3.5 49.8 1.0 C A:LEU15 3.7 50.8 1.0 N5 A:YXD301 3.8 30.9 1.0 CG1 A:VAL23 3.9 44.4 1.0 CB A:LEU15 3.9 44.7 1.0 C20 A:YXD301 3.9 36.9 1.0 CB A:VAL23 3.9 45.4 1.0 N A:GLY16 3.9 50.0 1.0 CA A:GLY16 4.1 51.2 1.0 C1 A:YXD301 4.1 31.3 1.0 C14 A:YXD301 4.3 43.1 1.0 O A:HOH482 4.4 39.3 1.0 CG2 A:VAL23 4.4 45.1 1.0 CA A:LEU15 4.4 45.1 1.0 C5 A:YXD301 4.4 45.7 1.0 C A:YXD301 4.5 28.4 1.0 C19 A:YXD301 4.7 34.9 1.0 O A:HOH508 4.7 44.7 1.0 C18 A:YXD301 4.8 31.2 1.0 N3 A:YXD301 4.9 38.6 1.0 C6 A:YXD301 4.9 46.8 1.0

Fluorine binding site 3 out of 3 in the Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of CHK1 10-Pt. Mutant Complex with LRRK2 Inhibitor 18 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:47.7 occ:1.00 F1 A:YXD301 0.0 47.7 1.0 C4 A:YXD301 1.3 46.5 1.0 F A:YXD301 2.1 47.1 1.0 F2 A:YXD301 2.1 47.5 1.0 C3 A:YXD301 2.4 43.1 1.0 N A:YXD301 2.8 35.4 1.0 C2 A:YXD301 3.0 41.1 1.0 O A:HOH482 3.2 39.3 1.0 CD2 A:LEU137 3.3 28.6 1.0 N1 A:YXD301 3.4 43.4 1.0 N5 A:YXD301 3.5 30.9 1.0 CD1 A:LEU137 3.5 27.8 1.0 C20 A:YXD301 3.7 36.9 1.0 O A:HOH508 3.8 44.7 1.0 C1 A:YXD301 3.9 31.3 1.0 CG A:LEU137 4.0 27.2 1.0 C A:YXD301 4.1 28.4 1.0 O A:HIS134 4.2 24.5 1.0 C14 A:YXD301 4.3 43.1 1.0 C18 A:YXD301 4.4 31.2 1.0 C19 A:YXD301 4.4 34.9 1.0 C5 A:YXD301 4.6 45.7 1.0 N3 A:YXD301 4.7 38.6 1.0 O A:YXD301 4.9 30.9 1.0 C6 A:YXD301 5.0 46.8 1.0

A.Gulati, C.S.Yeung, B.Lapointe, S.D.Kattar, H.Gunaydin, J.D.Scott, K.K.Childers, J.L.Methot, V.Simov, R.Kurukulasuriya, B.Pio, G.J.Morriello, P.Liu, H.Tang, S.Neelamkavil, H.B.Wood, V.L.Rada, M.J.Ardolino, X.C.Yan, R.Palte, K.Otte, R.Faltus, J.Woodhouse, L.G.Hegde, P.Ciaccio, E.C.Minnihan, E.F.Dimauro, M.J.Fell, P.H.Fuller, J.M.Ellis. Optimization of Brain-Penetrant Picolinamide Derived Leucine-Rich Repeat Kinase 2 (LRRK2) Inhibitors Rsc Med Chem 2021.
ISSN: ESSN 2632-8682
DOI: 10.1039/D1MD00097G