Fluorine in PDB 5i3y: Crystal Structure of BACE1 in Complex with Aminoquinoline Inhibitor 9

All present enzymatic activity of Crystal Structure of BACE1 in Complex with Aminoquinoline Inhibitor 9:
3.4.23.46;

The structure of Crystal Structure of BACE1 in Complex with Aminoquinoline Inhibitor 9, PDB code: 5i3y was solved by D.A.Whittington, A.M.Long, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.15
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.788, 102.788, 170.300, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 23.8

The binding sites of Fluorine atom in the Crystal Structure of BACE1 in Complex with Aminoquinoline Inhibitor 9 (pdb code 5i3y). 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 BACE1 in Complex with Aminoquinoline Inhibitor 9, PDB code: 5i3y:

Fluorine binding site 1 out of 1 in the Crystal Structure of BACE1 in Complex with Aminoquinoline Inhibitor 9


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 BACE1 in Complex with Aminoquinoline Inhibitor 9 within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:17.2 occ:1.00 F1 A:68K401 0.0 17.2 1.0 C36 A:68K401 1.3 16.9 1.0 C35 A:68K401 2.4 16.3 1.0 C37 A:68K401 2.4 16.8 1.0 CB A:ALA335 3.1 28.2 1.0 O A:HOH576 3.6 23.5 1.0 C38 A:68K401 3.6 17.4 1.0 C34 A:68K401 3.6 16.9 1.0 CE1 A:TYR14 3.8 18.7 1.0 OG1 A:THR232 4.0 32.4 1.0 CA A:THR232 4.1 29.3 1.0 C33 A:68K401 4.1 16.9 1.0 NH2 A:ARG307 4.2 55.0 1.0 CD1 A:TYR14 4.2 16.4 1.0 OE2 A:GLU339 4.3 33.5 1.0 O A:THR231 4.3 23.6 1.0 CB A:THR232 4.4 33.1 1.0 CA A:ALA335 4.6 26.3 1.0 CG2 A:THR232 4.6 35.5 1.0 N A:THR232 4.6 27.7 1.0 CA A:GLY13 4.6 17.4 1.0 C A:THR231 4.7 25.0 1.0 N A:GLY13 4.7 19.0 1.0 CZ A:TYR14 4.9 20.6 1.0 O A:SER229 4.9 15.9 1.0

J.B.Jordan, D.A.Whittington, M.D.Bartberger, E.A.Sickmier, K.Chen, Y.Cheng, T.Judd. Fragment-Linking Approach Using (19)F uc(Nmr) Spectroscopy to Obtain Highly Potent and Selective Inhibitors of Beta-Secretase. J.Med.Chem. V. 59 3732 2016.
ISSN: ISSN 0022-2623
PubMed: 26978477
DOI: 10.1021/ACS.JMEDCHEM.5B01917