Fluorine in PDB 4wtu: Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22

All present enzymatic activity of Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22:
3.4.23.46;

The structure of Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22, PDB code: 4wtu 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)	48.97 / 1.85
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.136, 102.136, 171.425, 90.00, 90.00, 120.00
R / Rfree (%)	16.9 / 19.6

The structure of Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22 also contains other interesting chemical elements:

Iodine

(I)

4 atoms

The binding sites of Fluorine atom in the Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22 (pdb code 4wtu). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22, PDB code: 4wtu:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22


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 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22 within 5.0Å range: probe atom residue distance (Å) B Occ A:F407 b:24.0 occ:1.00 F33 A:3UT407 0.0 24.0 1.0 C11 A:3UT407 1.3 20.4 1.0 N12 A:3UT407 2.3 21.9 1.0 C8 A:3UT407 2.3 21.1 1.0 O7 A:3UT407 2.6 19.4 1.0 NE1 A:TRP76 3.0 20.5 1.0 CD1 A:TRP76 3.1 20.6 1.0 O A:HOH676 3.2 19.1 1.0 CE1 A:TYR71 3.4 22.0 1.0 CE1 A:PHE108 3.4 20.0 1.0 CD1 A:TYR71 3.5 23.3 1.0 C13 A:3UT407 3.6 21.8 1.0 C9 A:3UT407 3.6 21.6 1.0 CD1 A:PHE108 3.7 18.4 1.0 C4 A:3UT407 4.0 21.1 1.0 CZ A:TYR71 4.0 22.3 1.0 C14 A:3UT407 4.1 22.3 1.0 CG A:TYR71 4.2 23.1 1.0 CD1 A:ILE118 4.3 16.7 1.0 CE2 A:TRP76 4.4 21.1 1.0 CG A:TRP76 4.5 19.2 1.0 CZ A:PHE108 4.5 20.3 1.0 CG1 A:VAL69 4.6 21.8 1.0 OH A:TYR71 4.6 25.2 1.0 CE2 A:TYR71 4.6 22.9 1.0 C20 A:3UT407 4.7 23.6 1.0 CD2 A:TYR71 4.7 21.1 1.0 C3 A:3UT407 4.8 20.2 1.0 C32 A:3UT407 4.9 23.4 1.0 C10 A:3UT407 4.9 24.5 1.0 CG2 A:ILE118 4.9 15.6 1.0 C5 A:3UT407 4.9 22.0 1.0 CG A:PHE108 5.0 19.2 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 3-Aza-4- Fluoro-Xanthene Inhibitor 22 within 5.0Å range: probe atom residue distance (Å) B Occ A:F407 b:23.4 occ:1.00 F27 A:3UT407 0.0 23.4 1.0 C22 A:3UT407 1.3 23.2 1.0 N23 A:3UT407 2.3 23.9 1.0 C21 A:3UT407 2.4 23.0 1.0 C1 A:3UT407 2.8 20.9 1.0 O A:GLY230 2.9 20.4 1.0 C6 A:3UT407 3.0 21.1 1.0 CA A:GLY230 3.1 20.6 1.0 C A:GLY230 3.3 21.0 1.0 CD2 A:LEU30 3.4 18.9 1.0 C24 A:3UT407 3.5 26.9 1.0 C26 A:3UT407 3.6 23.8 1.0 CD1 A:LEU30 3.7 17.9 1.0 O A:HOH635 3.8 30.4 1.0 C2 A:3UT407 3.9 20.9 1.0 CG A:LEU30 3.9 18.7 1.0 C25 A:3UT407 4.0 25.5 1.0 C5 A:3UT407 4.2 22.0 1.0 N A:GLY230 4.5 18.1 1.0 N A:THR231 4.5 19.5 1.0 O A:HOH660 4.5 21.7 1.0 O A:HOH709 4.6 25.6 1.0 O A:SER229 4.6 17.5 1.0 N18 A:3UT407 4.6 27.0 1.0 CA A:GLY13 4.7 21.8 1.0 C3 A:3UT407 4.8 20.2 1.0 C4 A:3UT407 4.9 21.1 1.0 C17 A:3UT407 5.0 27.8 1.0 C A:SER229 5.0 18.4 1.0

Y.Cheng, J.Brown, T.C.Judd, P.Lopez, W.Qian, T.S.Powers, J.J.Chen, M.D.Bartberger, K.Chen, R.T.Dunn, O.Epstein, R.T.Fremeau, S.Harried, D.Hickman, S.A.Hitchcock, Y.Luo, A.E.Minatti, V.F.Patel, H.M.Vargas, R.C.Wahl, M.M.Weiss, P.H.Wen, R.D.White, D.A.Whittington, X.M.Zheng, S.Wood. An Orally Available BACE1 Inhibitor That Affords Robust Cns A Beta Reduction Without Cardiovascular Liabilities. Acs Med.Chem.Lett. V. 6 210 2015.
ISSN: ISSN 1948-5875
PubMed: 25699151
DOI: 10.1021/ML500458T