Fluorine in PDB 5i2k: Structure of the Human GLUN1/GLUN2A Lbd in Complex with 7-{[Ethyl(4- Fluorophenyl)Amino]Methyl}-N,2-Dimethyl-5-Oxo-5H-[1,3]Thiazolo[3,2- A]Pyrimidine-3-Carboxamide (Compound 19)

The structure of Structure of the Human GLUN1/GLUN2A Lbd in Complex with 7-{[Ethyl(4- Fluorophenyl)Amino]Methyl}-N,2-Dimethyl-5-Oxo-5H-[1,3]Thiazolo[3,2- A]Pyrimidine-3-Carboxamide (Compound 19), PDB code: 5i2k was solved by H.J.A.Wallweber, P.J.Lupardus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.72 / 2.86
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.655, 89.329, 119.447, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 25.6

The binding sites of Fluorine atom in the Structure of the Human GLUN1/GLUN2A Lbd in Complex with 7-{[Ethyl(4- Fluorophenyl)Amino]Methyl}-N,2-Dimethyl-5-Oxo-5H-[1,3]Thiazolo[3,2- A]Pyrimidine-3-Carboxamide (Compound 19) (pdb code 5i2k). 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 Structure of the Human GLUN1/GLUN2A Lbd in Complex with 7-{[Ethyl(4- Fluorophenyl)Amino]Methyl}-N,2-Dimethyl-5-Oxo-5H-[1,3]Thiazolo[3,2- A]Pyrimidine-3-Carboxamide (Compound 19), PDB code: 5i2k:

Fluorine binding site 1 out of 1 in the Structure of the Human GLUN1/GLUN2A Lbd in Complex with 7-{[Ethyl(4- Fluorophenyl)Amino]Methyl}-N,2-Dimethyl-5-Oxo-5H-[1,3]Thiazolo[3,2- A]Pyrimidine-3-Carboxamide (Compound 19)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of the Human GLUN1/GLUN2A Lbd in Complex with 7-{[Ethyl(4- Fluorophenyl)Amino]Methyl}-N,2-Dimethyl-5-Oxo-5H-[1,3]Thiazolo[3,2- A]Pyrimidine-3-Carboxamide (Compound 19) within 5.0Å range: probe atom residue distance (Å) B Occ B:F302 b:32.3 occ:1.00 F26 B:67H302 0.0 32.3 1.0 C23 B:67H302 1.4 28.5 1.0 C24 B:67H302 2.3 28.7 1.0 C22 B:67H302 2.3 27.7 1.0 CD2 B:LEU270 3.0 21.1 1.0 CG2 A:ILE116 3.0 30.1 1.0 CD B:LYS140 3.1 40.3 1.0 CB A:ILE116 3.6 32.7 1.0 CG B:LYS140 3.6 40.2 1.0 C25 B:67H302 3.6 29.6 1.0 C21 B:67H302 3.6 29.1 1.0 CB B:LYS140 3.8 31.5 1.0 CD1 A:ILE116 3.8 35.7 1.0 OG1 A:THR242 3.9 34.7 1.0 C20 B:67H302 4.1 31.0 1.0 CE B:LYS140 4.1 43.2 1.0 CG B:LEU270 4.2 25.2 1.0 CG1 A:ILE116 4.2 33.2 1.0 CD1 B:LEU270 4.5 25.2 1.0 N A:GLY243 4.8 26.2 1.0 CD B:PRO141 4.9 31.4 1.0 CA A:ILE116 4.9 30.2 1.0 CA A:THR242 4.9 28.3 1.0 CA B:LYS140 4.9 29.5 1.0 CB A:THR242 4.9 39.5 1.0 O A:ILE116 5.0 38.2 1.0

M.Volgraf, B.D.Sellers, Y.Jiang, G.Wu, C.Q.Ly, E.Villemure, R.M.Pastor, P.W.Yuen, A.Lu, X.Luo, M.Liu, S.Zhang, L.Sun, Y.Fu, P.J.Lupardus, H.J.Wallweber, B.M.Liederer, G.Deshmukh, E.Plise, S.Tay, P.Reynen, J.Herrington, A.Gustafson, Y.Liu, A.Dirksen, M.G.Dietz, Y.Liu, T.M.Wang, J.E.Hanson, D.Hackos, K.Scearce-Levie, J.B.Schwarz. Discovery of GLUN2A-Selective Nmda Receptor Positive Allosteric Modulators (Pams): Tuning Deactivation Kinetics Via Structure-Based Design. J.Med.Chem. V. 59 2760 2016.
ISSN: ISSN 0022-2623
PubMed: 26919761
DOI: 10.1021/ACS.JMEDCHEM.5B02010