Fluorine in PDB 3l58: Structure of Bace Bound to SCH589432

All present enzymatic activity of Structure of Bace Bound to SCH589432:
3.4.23.46;

The structure of Structure of Bace Bound to SCH589432, PDB code: 3l58 was solved by C.Strickland, Z.Zhu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.72 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.455, 89.340, 131.172, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 22.3

The binding sites of Fluorine atom in the Structure of Bace Bound to SCH589432 (pdb code 3l58). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structure of Bace Bound to SCH589432, PDB code: 3l58:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Structure of Bace Bound to SCH589432


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Bace Bound to SCH589432 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:17.1 occ:1.00 F2 A:CS51 0.0 17.1 1.0 C23 A:CS51 1.3 15.8 1.0 C24 A:CS51 2.4 15.9 1.0 C22 A:CS51 2.4 13.1 1.0 CZ2 A:TRP176 3.4 10.6 1.0 C12 A:CS51 3.6 11.0 1.0 CD1 A:ILE171 3.6 15.5 1.0 C25 A:CS51 3.7 16.0 1.0 C21 A:CS51 3.7 11.0 1.0 CD2 A:LEU91 3.7 22.1 1.0 CH2 A:TRP176 3.8 11.1 1.0 C8 A:CS51 3.8 15.0 1.0 C13 A:CS51 3.9 13.9 1.0 O A:HOH979 4.2 16.4 1.0 C26 A:CS51 4.2 11.4 1.0 CG1 A:ILE171 4.4 14.3 1.0 O A:PHE169 4.4 12.8 1.0 N1 A:CS51 4.4 13.8 1.0 C11 A:CS51 4.5 12.0 1.0 CE2 A:TRP176 4.5 11.7 1.0 C9 A:CS51 4.5 14.9 1.0 O A:GLY291 4.7 8.0 1.0 F1 A:CS51 4.8 18.4 1.0 O A:GLN73 4.8 11.9 1.0 NE2 A:GLN134 4.8 45.1 1.0 C17 A:CS51 4.9 9.7 1.0

Fluorine binding site 2 out of 4 in the Structure of Bace Bound to SCH589432


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Bace Bound to SCH589432 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:18.4 occ:1.00 F1 A:CS51 0.0 18.4 1.0 C25 A:CS51 1.3 16.0 1.0 C26 A:CS51 2.4 11.4 1.0 C24 A:CS51 2.4 15.9 1.0 O A:GLN134 3.1 28.2 1.0 NE2 A:GLN134 3.2 45.1 1.0 CD1 A:PHE169 3.2 12.7 1.0 CA A:GLY135 3.3 16.8 1.0 CD2 A:TYR132 3.6 13.7 1.0 C21 A:CS51 3.7 11.0 1.0 C23 A:CS51 3.7 15.8 1.0 C A:GLY135 3.8 16.1 1.0 O A:LYS168 3.8 17.2 1.0 CA A:PHE169 3.8 13.3 1.0 CE1 A:PHE169 4.0 12.4 1.0 C A:GLN134 4.0 27.9 1.0 CD A:GLN134 4.1 42.6 1.0 N A:GLY135 4.1 22.7 1.0 CG A:PHE169 4.2 11.8 1.0 C22 A:CS51 4.2 13.1 1.0 O A:GLY135 4.2 14.3 1.0 O A:HOH979 4.2 16.4 1.0 CB A:PHE169 4.2 12.0 1.0 CE2 A:TYR132 4.3 14.3 1.0 CG A:TYR132 4.3 12.1 1.0 N A:LYS136 4.3 16.4 1.0 OE1 A:GLN134 4.4 44.2 1.0 O A:PHE169 4.4 12.8 1.0 CB A:TYR132 4.4 13.1 1.0 C A:LYS168 4.6 16.5 1.0 C A:PHE169 4.6 13.4 1.0 N A:PHE169 4.7 14.1 1.0 F2 A:CS51 4.8 17.1 1.0 C17 A:CS51 4.9 9.7 1.0

Fluorine binding site 3 out of 4 in the Structure of Bace Bound to SCH589432


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of Bace Bound to SCH589432 within 5.0Å range: probe atom residue distance (Å) B Occ B:F1 b:12.9 occ:1.00 F2 B:CS51 0.0 12.9 1.0 C23 B:CS51 1.3 14.1 1.0 C22 B:CS51 2.4 12.7 1.0 C24 B:CS51 2.4 12.9 1.0 CZ2 B:TRP176 3.4 10.5 1.0 C12 B:CS51 3.5 13.6 1.0 CD1 B:ILE171 3.6 13.3 1.0 CD2 B:LEU91 3.7 19.3 1.0 C21 B:CS51 3.7 11.5 1.0 C25 B:CS51 3.7 15.8 1.0 C8 B:CS51 3.7 15.5 1.0 CH2 B:TRP176 3.8 10.8 1.0 C13 B:CS51 3.9 15.7 1.0 C26 B:CS51 4.2 10.5 1.0 O B:HOH958 4.2 17.4 1.0 O B:PHE169 4.3 12.9 1.0 CG1 B:ILE171 4.3 14.2 1.0 N1 B:CS51 4.4 14.3 1.0 C9 B:CS51 4.5 17.0 1.0 C11 B:CS51 4.5 12.9 1.0 CE2 B:TRP176 4.5 10.7 1.0 O B:GLY291 4.7 8.2 1.0 OE1 B:GLN134 4.7 42.7 1.0 F1 B:CS51 4.8 20.9 1.0 C17 B:CS51 4.9 9.1 1.0 O B:GLN73 4.9 12.6 1.0

Fluorine binding site 4 out of 4 in the Structure of Bace Bound to SCH589432


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of Bace Bound to SCH589432 within 5.0Å range: probe atom residue distance (Å) B Occ B:F1 b:20.9 occ:1.00 F1 B:CS51 0.0 20.9 1.0 C25 B:CS51 1.3 15.8 1.0 C26 B:CS51 2.4 10.5 1.0 C24 B:CS51 2.4 12.9 1.0 O B:GLN134 3.1 31.0 1.0 OE1 B:GLN134 3.2 42.7 1.0 CA B:GLY135 3.2 18.6 1.0 CD1 B:PHE169 3.3 11.3 1.0 C21 B:CS51 3.7 11.5 1.0 C23 B:CS51 3.7 14.1 1.0 C B:GLY135 3.7 13.3 1.0 O B:LYS168 3.7 13.8 1.0 CD2 B:TYR132 3.7 13.5 1.0 CA B:PHE169 3.8 12.8 1.0 C B:GLN134 3.9 29.6 1.0 CD B:GLN134 4.0 39.4 1.0 CE1 B:PHE169 4.1 12.3 1.0 N B:GLY135 4.1 23.8 1.0 O B:GLY135 4.1 11.8 1.0 C22 B:CS51 4.2 12.7 1.0 CG B:PHE169 4.2 10.9 1.0 N B:LYS136 4.2 13.9 1.0 CB B:PHE169 4.3 11.4 1.0 O B:HOH958 4.3 17.4 1.0 NE2 B:GLN134 4.3 39.5 1.0 CE2 B:TYR132 4.3 13.8 1.0 O B:PHE169 4.4 12.9 1.0 CG B:TYR132 4.4 11.7 1.0 CB B:TYR132 4.5 10.2 1.0 C B:LYS168 4.5 15.7 1.0 C B:PHE169 4.6 13.1 1.0 N B:PHE169 4.6 13.9 1.0 F2 B:CS51 4.8 12.9 1.0 C17 B:CS51 4.9 9.1 1.0

Z.Zhu, Z.Y.Sun, Y.Ye, J.Voigt, C.Strickland, E.M.Smith, J.Cumming, L.Wang, J.Wong, Y.S.Wang, D.F.Wyss, X.Chen, R.Kuvelkar, M.E.Kennedy, L.Favreau, E.Parker, B.A.Mckittrick, A.Stamford, M.Czarniecki, W.Greenlee, J.C.Hunter. Discovery of Cyclic Acylguanidines As Highly Potent and Selective Beta-Site Amyloid Cleaving Enzyme (Bace) Inhibitors: Part I-Inhibitor Design and Validation J.Med.Chem. V. 53 951 2010.
ISSN: ISSN 0022-2623
PubMed: 20043696
DOI: 10.1021/JM901408P