Fluorine in PDB 6n6o: Crystal Structure of the Human Ttk in Complex with An Inhibitor

All present enzymatic activity of Crystal Structure of the Human Ttk in Complex with An Inhibitor:
2.7.12.1;

The structure of Crystal Structure of the Human Ttk in Complex with An Inhibitor, PDB code: 6n6o was solved by G.Fenalti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	61.84 / 2.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	71.410, 71.410, 122.491, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 24.4

The structure of Crystal Structure of the Human Ttk in Complex with An Inhibitor also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of the Human Ttk in Complex with An Inhibitor (pdb code 6n6o). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of the Human Ttk in Complex with An Inhibitor, PDB code: 6n6o:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of the Human Ttk in Complex with An Inhibitor


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 the Human Ttk in Complex with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F801 b:61.4 occ:1.00 F2 A:KE7801 0.0 61.4 1.0 C25 A:KE7801 1.3 60.5 1.0 F1 A:KE7801 2.2 68.7 1.0 F3 A:KE7801 2.2 52.2 1.0 C23 A:KE7801 2.3 56.1 1.0 O4 A:KE7801 2.7 57.7 1.0 C24 A:KE7801 2.8 54.0 1.0 NE2 A:GLN541 2.8 52.9 1.0 CD A:GLN541 3.2 55.4 1.0 CD1 A:ILE531 3.4 59.1 1.0 CG1 A:ILE531 3.6 58.4 1.0 CG A:GLN541 3.6 59.0 1.0 CB A:GLN541 3.7 54.9 1.0 C19 A:KE7801 3.8 51.0 1.0 OE1 A:GLN541 3.9 46.6 1.0 SG A:CYS604 3.9 61.2 1.0 C18 A:KE7801 4.4 42.8 1.0 C14 A:KE7801 4.7 51.6 1.0 N4 A:KE7801 4.7 57.0 1.0 CD A:LYS529 4.8 71.5 1.0 CA A:GLN541 4.9 53.9 1.0 CB A:ILE531 4.9 50.0 1.0 CE A:LYS529 4.9 79.0 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of the Human Ttk in Complex with An Inhibitor


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 the Human Ttk in Complex with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F801 b:52.2 occ:1.00 F3 A:KE7801 0.0 52.2 1.0 C25 A:KE7801 1.3 60.5 1.0 F1 A:KE7801 2.2 68.7 1.0 F2 A:KE7801 2.2 61.4 1.0 C23 A:KE7801 2.3 56.1 1.0 O4 A:KE7801 2.8 57.7 1.0 C18 A:KE7801 3.0 42.8 1.0 C19 A:KE7801 3.1 51.0 1.0 CG1 A:ILE531 3.5 58.4 1.0 C24 A:KE7801 3.7 54.0 1.0 NZ A:LYS529 4.0 85.5 1.0 CE A:LYS529 4.0 79.0 1.0 CD1 A:ILE531 4.1 59.1 1.0 C17 A:KE7801 4.1 45.5 1.0 CG2 A:ILE531 4.2 50.1 1.0 C14 A:KE7801 4.3 51.6 1.0 CB A:ILE531 4.4 50.0 1.0 CD A:LYS529 4.5 71.5 1.0 NE2 A:GLN541 4.7 52.9 1.0 CA A:ILE531 4.7 52.0 1.0 C20 A:KE7801 4.8 46.6 1.0 N4 A:KE7801 5.0 57.0 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of the Human Ttk in Complex with An Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the Human Ttk in Complex with An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F801 b:68.7 occ:1.00 F1 A:KE7801 0.0 68.7 1.0 C25 A:KE7801 1.3 60.5 1.0 F2 A:KE7801 2.2 61.4 1.0 F3 A:KE7801 2.2 52.2 1.0 C23 A:KE7801 2.3 56.1 1.0 C24 A:KE7801 2.8 54.0 1.0 NE2 A:GLN541 3.3 52.9 1.0 O4 A:KE7801 3.5 57.7 1.0 CD A:GLN541 3.9 55.4 1.0 OE1 A:GLN541 4.1 46.6 1.0 CD A:LYS529 4.3 71.5 1.0 C19 A:KE7801 4.4 51.0 1.0 NZ A:LYS529 4.4 85.5 1.0 C18 A:KE7801 4.4 42.8 1.0 CE A:LYS529 4.5 79.0 1.0 CG A:GLN541 4.9 59.0 1.0

J.R.Riggs, J.Elsner, D.Cashion, D.Robinson, L.Tehrani, M.Nagy, K.E.Fultz, R.Krishna Narla, X.Peng, T.Tran, A.Kulkarni, S.Bahmanyar, K.Condroski, B.Pagarigan, G.Fenalti, L.Lebrun, K.Leftheris, D.Zhu, J.F.Boylan. Design and Optimization Leading to An Orally Active Ttk Protein Kinase Inhibitor with Robust Single Agent Efficacy. J.Med.Chem. V. 62 4401 2019.
ISSN: ISSN 0022-2623
PubMed: 30998356
DOI: 10.1021/ACS.JMEDCHEM.8B01869