Fluorine in PDB 2qk5: Structure of BACE1 Bound to SCH626485

All present enzymatic activity of Structure of BACE1 Bound to SCH626485:
3.4.23.46;

The structure of Structure of BACE1 Bound to SCH626485, PDB code: 2qk5 was solved by C.O.Strickland, U.Iserloh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.485, 89.204, 131.147, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 22.9

The binding sites of Fluorine atom in the Structure of BACE1 Bound to SCH626485 (pdb code 2qk5). 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 BACE1 Bound to SCH626485, PDB code: 2qk5:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Structure of BACE1 Bound to SCH626485


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of BACE1 Bound to SCH626485 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:14.7 occ:1.00 F2 A:CS51 0.0 14.7 1.0 C23 A:CS51 1.3 9.8 1.0 C24 A:CS51 2.4 9.7 1.0 C22 A:CS51 2.4 8.4 1.0 CZ2 A:TRP176 3.5 10.5 1.0 CD2 A:LEU91 3.6 12.5 1.0 C13 A:CS51 3.6 5.3 1.0 C8 A:CS51 3.6 8.5 1.0 C25 A:CS51 3.7 11.2 1.0 C21 A:CS51 3.7 9.3 1.0 CD1 A:ILE171 3.8 17.1 1.0 CH2 A:TRP176 3.9 9.9 1.0 C12 A:CS51 3.9 11.4 1.0 C26 A:CS51 4.2 8.1 1.0 O A:HOH983 4.2 14.1 1.0 C9 A:CS51 4.3 8.9 1.0 N1 A:CS51 4.4 11.1 1.0 CG1 A:ILE171 4.5 17.4 1.0 O A:PHE169 4.5 12.7 1.0 C11 A:CS51 4.6 10.2 1.0 CE2 A:TRP176 4.7 11.2 1.0 O A:GLY291 4.7 7.3 1.0 F1 A:CS51 4.8 15.8 1.0 C17 A:CS51 4.9 9.2 1.0 O A:GLN73 4.9 12.6 1.0

Fluorine binding site 2 out of 4 in the Structure of BACE1 Bound to SCH626485


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of BACE1 Bound to SCH626485 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:15.8 occ:1.00 F1 A:CS51 0.0 15.8 1.0 C25 A:CS51 1.3 11.2 1.0 C24 A:CS51 2.4 9.7 1.0 C26 A:CS51 2.4 8.1 1.0 O A:GLN134 3.0 34.1 1.0 CD1 A:PHE169 3.3 10.6 1.0 CA A:GLY135 3.4 18.8 1.0 C23 A:CS51 3.7 9.8 1.0 C21 A:CS51 3.7 9.3 1.0 O A:LYS168 3.8 16.6 1.0 CD2 A:TYR132 3.8 13.6 1.0 CA A:PHE169 3.8 9.8 1.0 C A:GLY135 3.9 17.6 1.0 C A:GLN134 4.0 33.1 1.0 CE1 A:PHE169 4.0 9.6 1.0 O A:HOH983 4.1 14.1 1.0 C22 A:CS51 4.2 8.4 1.0 O A:GLY135 4.2 14.2 1.0 CG A:PHE169 4.2 10.5 1.0 N A:GLY135 4.2 26.2 1.0 CB A:PHE169 4.3 9.2 1.0 CG A:TYR132 4.4 13.1 1.0 O A:PHE169 4.4 12.7 1.0 CB A:TYR132 4.4 11.3 1.0 CE2 A:TYR132 4.5 11.9 1.0 N A:LYS136 4.5 17.1 1.0 C A:LYS168 4.6 18.6 1.0 C A:PHE169 4.6 13.0 1.0 N A:PHE169 4.7 14.1 1.0 F2 A:CS51 4.8 14.7 1.0 C17 A:CS51 4.9 9.2 1.0 O2 A:CS51 5.0 9.5 1.0

Fluorine binding site 3 out of 4 in the Structure of BACE1 Bound to SCH626485


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of BACE1 Bound to SCH626485 within 5.0Å range: probe atom residue distance (Å) B Occ B:F1 b:12.0 occ:1.00 F2 B:CS51 0.0 12.0 1.0 C23 B:CS51 1.3 9.6 1.0 C22 B:CS51 2.4 7.4 1.0 C24 B:CS51 2.4 7.5 1.0 CZ2 B:TRP176 3.5 9.9 1.0 CD1 B:LEU91 3.5 19.9 1.0 C8 B:CS51 3.6 8.7 1.0 C21 B:CS51 3.7 8.4 1.0 C25 B:CS51 3.7 9.1 1.0 C13 B:CS51 3.7 13.0 1.0 CD1 B:ILE171 3.8 13.2 1.0 CH2 B:TRP176 3.8 8.7 1.0 C12 B:CS51 3.9 15.8 1.0 C26 B:CS51 4.2 5.6 1.0 C9 B:CS51 4.3 11.6 1.0 O B:PHE169 4.4 11.5 1.0 N1 B:CS51 4.4 10.9 1.0 CG1 B:ILE171 4.4 13.9 1.0 O B:HOH945 4.4 13.6 1.0 C11 B:CS51 4.7 13.7 1.0 O B:GLY291 4.7 12.2 1.0 CE2 B:TRP176 4.7 8.7 1.0 F1 B:CS51 4.8 13.2 1.0 C17 B:CS51 4.9 7.8 1.0 CG B:LEU91 5.0 14.5 1.0

Fluorine binding site 4 out of 4 in the Structure of BACE1 Bound to SCH626485


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of BACE1 Bound to SCH626485 within 5.0Å range: probe atom residue distance (Å) B Occ B:F1 b:13.2 occ:1.00 F1 B:CS51 0.0 13.2 1.0 C25 B:CS51 1.3 9.1 1.0 C24 B:CS51 2.4 7.5 1.0 C26 B:CS51 2.4 5.6 1.0 O B:GLN134 2.8 33.3 1.0 CA B:GLY135 3.3 19.7 1.0 CD1 B:PHE169 3.3 7.6 1.0 O B:LYS168 3.7 12.4 1.0 C23 B:CS51 3.7 9.6 1.0 C21 B:CS51 3.7 8.4 1.0 C B:GLY135 3.7 16.1 1.0 C B:GLN134 3.8 31.5 1.0 CA B:PHE169 3.8 8.7 1.0 CD2 B:TYR132 3.9 11.2 1.0 N B:GLY135 4.0 23.7 1.0 CE1 B:PHE169 4.1 7.8 1.0 O B:GLY135 4.1 15.7 1.0 C22 B:CS51 4.2 7.4 1.0 CG B:PHE169 4.2 9.0 1.0 N B:LYS136 4.3 15.8 1.0 CB B:PHE169 4.3 7.3 1.0 CG B:TYR132 4.3 10.6 1.0 O B:HOH945 4.4 13.6 1.0 CB B:TYR132 4.4 6.3 1.0 O B:PHE169 4.4 11.5 1.0 C B:LYS168 4.5 14.0 1.0 CE2 B:TYR132 4.5 7.2 1.0 C B:PHE169 4.6 12.1 1.0 N B:PHE169 4.6 11.9 1.0 F2 B:CS51 4.8 12.0 1.0 O2 B:CS51 4.9 8.4 1.0 C17 B:CS51 4.9 7.8 1.0

U.Iserloh, Y.Wu, J.N.Cumming, J.Pan, L.Y.Wang, A.W.Stamford, M.E.Kennedy, R.Kuvelkar, X.Chen, E.M.Parker, C.Strickland, J.Voigt. Potent Pyrrolidine- and Piperidine-Based Bace-1 Inhibitors. Bioorg.Med.Chem.Lett. V. 18 414 2008.
ISSN: ISSN 0960-894X
PubMed: 18023580
DOI: 10.1016/J.BMCL.2007.10.116