Chlorine in PDB 6rz7: Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2570366 (F222 Space Group)

The structure of Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2570366 (F222 Space Group), PDB code: 6rz7 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)	19.93 / 2.43
Space group	F 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	81.830, 142.070, 171.160, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 25.9

The structure of Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2570366 (F222 Space Group) also contains other interesting chemical elements:

Fluorine

(F)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2570366 (F222 Space Group) (pdb code 6rz7). 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 the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2570366 (F222 Space Group), PDB code: 6rz7:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2570366 (F222 Space Group)


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 the Human Cysteinyl Leukotriene Receptor 2 in Complex with Ono-2570366 (F222 Space Group) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl2001 b:48.9 occ:1.00 CL1 A:KNW2001 0.0 48.9 1.0 C27 A:KNW2001 1.7 46.4 1.0 C26 A:KNW2001 2.7 45.1 1.0 C22 A:KNW2001 2.7 45.0 1.0 C21 A:KNW2001 3.0 45.0 1.0 C20 A:KNW2001 3.6 44.8 1.0 CG2 A:ILE204 3.7 46.0 1.0 C25 A:KNW2001 4.0 44.2 1.0 C23 A:KNW2001 4.0 44.3 1.0 CB A:ILE204 4.1 45.8 1.0 N A:ALA205 4.2 40.9 1.0 CB A:SER169 4.3 42.4 1.0 CE A:MET201 4.3 83.2 1.0 CA A:ALA205 4.4 41.3 1.0 C24 A:KNW2001 4.5 44.4 1.0 O A:SER169 4.5 41.1 1.0 CB A:ALA205 4.5 41.6 1.0 C A:ILE204 4.5 41.8 1.0 C19 A:KNW2001 4.6 44.6 1.0 O A:MET201 4.6 53.9 1.0 OG A:SER169 4.9 42.7 1.0 O A:ILE204 4.9 40.6 1.0 CD1 A:ILE204 4.9 46.3 1.0 CA A:ILE204 5.0 44.7 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