Fluorine in PDB 4fat: Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator

The structure of Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator, PDB code: 4fat was solved by J.K.F.Maclean, B.Kazemier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.40
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	63.866, 88.143, 47.391, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 20.9

The binding sites of Fluorine atom in the Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator (pdb code 4fat). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator, PDB code: 4fat:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator within 5.0Å range: probe atom residue distance (Å) B Occ A:F302 b:18.7 occ:0.50 F21 A:496302 0.0 18.7 0.5 C20 A:496302 1.3 18.9 0.5 F22 A:496302 2.1 20.9 0.5 F23 A:496302 2.2 19.9 0.5 C19 A:496302 2.3 13.6 0.5 O29 A:496302 3.2 13.6 0.2 N18 A:496302 3.2 13.6 0.5 C25 A:496302 3.2 13.3 0.5 CB A:LYS218 3.5 10.9 1.0 N A:GLY219 3.6 8.8 1.0 CA A:LYS218 3.6 10.5 1.0 C26 A:496302 3.7 12.6 0.5 C A:LYS218 3.9 9.6 1.0 CB A:ILE92 3.9 9.6 1.0 O A:ILE92 4.0 10.7 1.0 CG2 A:ILE92 4.2 12.2 1.0 N17 A:496302 4.3 13.1 0.5 C24 A:496302 4.3 13.2 0.5 O A:GLY219 4.4 9.4 1.0 CA A:GLY219 4.4 9.4 1.0 CD1 A:ILE92 4.6 10.7 1.0 C A:ILE92 4.8 10.6 1.0 CG1 A:ILE92 4.8 9.8 1.0 CA A:ILE92 4.9 9.4 1.0 C A:GLY219 4.9 9.2 1.0 CG A:LYS218 4.9 11.0 1.0 O29 A:496302 4.9 11.9 0.2 O A:SER217 4.9 12.0 1.0 O A:LYS218 5.0 9.9 1.0 N A:LYS218 5.0 10.1 1.0

Fluorine binding site 2 out of 3 in the Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator within 5.0Å range: probe atom residue distance (Å) B Occ A:F302 b:20.9 occ:0.50 F22 A:496302 0.0 20.9 0.5 C20 A:496302 1.3 18.9 0.5 F23 A:496302 2.0 19.9 0.5 F21 A:496302 2.1 18.7 0.5 C19 A:496302 2.3 13.6 0.5 C25 A:496302 2.8 13.3 0.5 C26 A:496302 2.9 12.6 0.5 O29 A:496302 3.0 13.6 0.2 N18 A:496302 3.5 13.6 0.5 O29 A:496302 3.7 11.9 0.2 C24 A:496302 4.1 13.2 0.5 N17 A:496302 4.4 13.1 0.5 CG2 A:ILE92 4.8 12.2 1.0

Fluorine binding site 3 out of 3 in the Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Ligand-Binding Domain of GLUA2 (Flip) Ionotropic Glutamate Receptor in Complex with An Allosteric Modulator within 5.0Å range: probe atom residue distance (Å) B Occ A:F302 b:19.9 occ:0.50 F23 A:496302 0.0 19.9 0.5 C20 A:496302 1.3 18.9 0.5 F22 A:496302 2.0 20.9 0.5 F21 A:496302 2.2 18.7 0.5 C19 A:496302 2.3 13.6 0.5 N18 A:496302 2.8 13.6 0.5 C25 A:496302 3.6 13.3 0.5 CD1 A:ILE92 3.6 10.7 1.0 CG A:PRO105 4.0 12.9 1.0 CG2 A:ILE92 4.1 12.2 1.0 N17 A:496302 4.1 13.1 0.5 CB A:ILE92 4.2 9.6 1.0 C26 A:496302 4.4 12.6 0.5 CD A:PRO105 4.4 11.6 1.0 C24 A:496302 4.5 13.2 0.5 CG1 A:ILE92 4.5 9.8 1.0 O29 A:496302 4.5 13.6 0.2 N A:GLY219 4.7 8.8 1.0 CB A:PRO105 4.8 11.6 1.0 CA A:GLY219 4.9 9.4 1.0

J.E.Harms, M.Benveniste, J.K.Maclean, K.M.Partin, C.Jamieson. Functional Analysis of A Novel Positive Allosteric Modulator of Ampa Receptors Derived From A Structure-Based Drug Design Strategy. Neuropharmacology V. 64 45 2013.
ISSN: ISSN 0028-3908
PubMed: 22735771
DOI: 10.1016/J.NEUROPHARM.2012.06.008