Fluorine in PDB 4rcf: Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 4- Fluoroxanthene Inhibitor 49

All present enzymatic activity of Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 4- Fluoroxanthene Inhibitor 49:
3.4.23.46;

The structure of Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 4- Fluoroxanthene Inhibitor 49, PDB code: 4rcf 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 / 1.78
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.262, 102.262, 170.306, 90.00, 90.00, 120.00
R / Rfree (%)	20.3 / 22.9

The structure of Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 4- Fluoroxanthene Inhibitor 49 also contains other interesting chemical elements:

Iodine

(I)

3 atoms

The binding sites of Fluorine atom in the Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 4- Fluoroxanthene Inhibitor 49 (pdb code 4rcf). 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 4- Fluoroxanthene Inhibitor 49, PDB code: 4rcf:
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 4- Fluoroxanthene Inhibitor 49


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 4- Fluoroxanthene Inhibitor 49 within 5.0Å range: probe atom residue distance (Å) B Occ A:F404 b:23.3 occ:1.00 F1 A:3LO404 0.0 23.3 1.0 C10 A:3LO404 1.3 20.9 1.0 C7 A:3LO404 2.3 19.4 1.0 C11 A:3LO404 2.4 21.5 1.0 O1 A:3LO404 2.7 19.7 1.0 CD1 A:TRP76 3.0 20.8 1.0 NE1 A:TRP76 3.0 20.0 1.0 CE1 A:TYR71 3.2 24.3 1.0 CD1 A:TYR71 3.4 23.9 1.0 CE1 A:PHE108 3.4 17.5 1.0 O A:HOH575 3.5 29.9 1.0 C8 A:3LO404 3.6 18.2 1.0 C12 A:3LO404 3.6 21.9 1.0 CD1 A:PHE108 3.6 17.8 1.0 CZ A:TYR71 3.9 23.6 1.0 C4 A:3LO404 4.0 18.1 1.0 CG A:TYR71 4.1 23.0 1.0 C13 A:3LO404 4.1 19.0 1.0 CE2 A:TRP76 4.3 20.7 1.0 CG A:TRP76 4.3 18.5 1.0 OH A:TYR71 4.5 24.0 1.0 CZ A:PHE108 4.5 18.8 1.0 CE2 A:TYR71 4.5 22.8 1.0 CD1 A:ILE118 4.5 16.1 1.0 CG1 A:VAL69 4.6 22.1 1.0 CD2 A:TYR71 4.6 22.1 1.0 C15 A:3LO404 4.8 24.0 1.0 C3 A:3LO404 4.8 18.7 1.0 C9 A:3LO404 4.9 18.4 1.0 CG A:PHE108 4.9 16.7 1.0 CB A:TYR71 4.9 23.9 1.0 O A:VAL69 4.9 21.9 1.0 C5 A:3LO404 5.0 17.7 1.0 C25 A:3LO404 5.0 28.7 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of BACE1 in Complex with 2-Aminooxazoline 4- Fluoroxanthene Inhibitor 49


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 4- Fluoroxanthene Inhibitor 49 within 5.0Å range: probe atom residue distance (Å) B Occ A:F404 b:20.7 occ:1.00 F2 A:3LO404 0.0 20.7 1.0 C18 A:3LO404 1.3 19.4 1.0 N3 A:3LO404 2.3 20.6 1.0 C14 A:3LO404 2.4 19.3 1.0 O A:GLY230 2.8 18.9 1.0 C1 A:3LO404 2.8 17.6 1.0 CA A:GLY230 3.0 18.0 1.0 C6 A:3LO404 3.0 17.2 1.0 C A:GLY230 3.1 18.8 1.0 CD2 A:LEU30 3.4 17.0 1.0 C19 A:3LO404 3.5 22.1 1.0 C21 A:3LO404 3.6 21.3 1.0 CD1 A:LEU30 3.6 18.0 1.0 O A:HOH547 3.6 24.9 1.0 CG A:LEU30 3.9 17.5 1.0 C2 A:3LO404 3.9 18.3 1.0 C20 A:3LO404 4.0 20.6 1.0 C5 A:3LO404 4.2 17.7 1.0 N A:GLY230 4.3 16.6 1.0 N A:THR231 4.3 18.2 1.0 O A:SER229 4.5 15.7 1.0 O A:HOH564 4.5 24.2 1.0 O A:HOH517 4.6 19.5 1.0 CA A:GLY13 4.7 21.5 1.0 N1 A:3LO404 4.7 18.6 1.0 C17 A:3LO404 4.9 18.3 1.0 C A:SER229 4.9 16.3 1.0 C3 A:3LO404 4.9 18.7 1.0 C4 A:3LO404 5.0 18.1 1.0

O.Epstein, M.C.Bryan, A.C.Cheng, K.Derakhchan, T.A.Dineen, D.Hickman, Z.Hua, J.B.Human, C.Kreiman, I.E.Marx, M.M.Weiss, R.C.Wahl, P.H.Wen, D.A.Whittington, S.Wood, X.M.Zheng, R.T.Fremeau, R.D.White, V.F.Patel. Lead Optimization and Modulation of Herg Activity in A Series of Aminooxazoline Xanthene Beta-Site Amyloid Precursor Protein Cleaving Enzyme (BACE1) Inhibitors. J.Med.Chem. 2014.
ISSN: ISSN 0022-2623
PubMed: 25389560
DOI: 10.1021/JM501266W