Fluorine in PDB 6rz9: Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2770372

The structure of Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2770372, PDB code: 6rz9 was solved by A.Gusach, A.Luginina, E.Marin, R.L.Brouillette, E.Besserer-Offroy, J.M.Longpre, A.Ishchenko, P.Popov, T.Fujimoto, T.Maruyama, B.Stauch, M.Ergasheva, D.Romanovskaya, A.Stepko, K.Kovalev, M.Shevtsov, V.Gordeliy, G.W.Han, P.Sarret, V.Katritch, V.Borshchevskiy, A.Mishin, V.Cherezov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.81 / 2.73
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	69.630, 170.210, 85.740, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 25.4

The binding sites of Fluorine atom in the Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2770372 (pdb code 6rz9). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2770372, PDB code: 6rz9:

Fluorine binding site 1 out of 1 in the Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2770372


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 Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2770372 within 5.0Å range: probe atom residue distance (Å) B Occ A:F2001 b:77.9 occ:1.00 F1 A:KO52001 0.0 77.9 1.0 C24 A:KO52001 1.4 70.9 1.0 C25 A:KO52001 2.3 79.7 1.0 C23 A:KO52001 2.3 69.6 1.0 CB A:TYR123 3.6 56.2 1.0 C26 A:KO52001 3.6 70.7 1.0 C22 A:KO52001 3.6 70.2 1.0 CE2 A:TYR127 3.7 56.3 1.0 C14 A:OLC2014 3.7 80.3 1.0 CA A:GLY209 3.8 45.4 1.0 CG A:TYR123 3.8 50.8 1.0 CD1 A:TYR123 4.0 58.1 1.0 C27 A:KO52001 4.1 70.1 1.0 CD2 A:TYR127 4.3 50.5 1.0 CG1 A:ILE166 4.3 56.1 1.0 N A:GLY209 4.4 49.7 1.0 C15 A:OLC2014 4.4 0.4 1.0 C17 A:OLC2014 4.6 0.0 1.0 CZ A:TYR127 4.6 54.7 1.0 CD2 A:TYR123 4.7 47.8 1.0 CD1 A:ILE166 4.7 80.0 1.0 OH A:TYR127 4.7 57.6 1.0 O A:VAL208 4.7 59.7 1.0 C A:VAL208 4.8 46.3 1.0 C16 A:OLC2014 4.8 0.2 1.0 CE1 A:TYR123 4.9 52.9 1.0 CA A:TYR123 4.9 58.4 1.0 C21 A:KO52001 4.9 71.0 1.0 C13 A:OLC2014 4.9 66.7 1.0 C A:GLY209 5.0 66.8 1.0

A.Gusach, A.Luginina, E.Marin, R.L.Brouillette, E.Besserer-Offroy, J.M.Longpre, A.Ishchenko, P.Popov, N.Patel, T.Fujimoto, T.Maruyama, B.Stauch, M.Ergasheva, D.Romanovskaia, A.Stepko, K.Kovalev, M.Shevtsov, V.Gordeliy, G.W.Han, V.Katritch, V.Borshchevskiy, P.Sarret, A.Mishin, V.Cherezov. Structural Basis of Ligand Selectivity and Disease Mutations in Cysteinyl Leukotriene Receptors. Nat Commun V. 10 5573 2019.
ISSN: ESSN 2041-1723
PubMed: 31811124
DOI: 10.1038/S41467-019-13348-2