Fluorine in PDB 5enk: Compound 18

All present enzymatic activity of Compound 18:
3.4.23.46;

The structure of Compound 18, PDB code: 5enk was solved by H.A.Lewis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	88.39 / 2.11
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	101.924, 101.924, 171.025, 90.00, 90.00, 120.00
R / Rfree (%)	23.3 / 25.4

The structure of Compound 18 also contains other interesting chemical elements:

Iodine

(I)

1 atom

The binding sites of Fluorine atom in the Compound 18 (pdb code 5enk). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Compound 18, PDB code: 5enk:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Compound 18


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Compound 18 within 5.0Å range: probe atom residue distance (Å) B Occ A:F503 b:23.4 occ:1.00 F22 A:5QV503 0.0 23.4 1.0 C21 A:5QV503 1.3 23.5 1.0 C20 A:5QV503 2.3 23.4 1.0 C16 A:5QV503 2.4 23.6 1.0 C15 A:5QV503 2.9 23.8 1.0 C10 A:5QV503 2.9 23.8 1.0 CE1 A:PHE156 3.1 20.2 1.0 C9 A:5QV503 3.1 24.1 1.0 CD1 A:PHE156 3.2 20.3 1.0 CE2 A:TYR119 3.2 31.3 1.0 O A:HOH661 3.4 30.5 1.0 C19 A:5QV503 3.6 23.7 1.0 CZ A:TYR119 3.6 31.3 1.0 C17 A:5QV503 3.7 23.6 1.0 CD2 A:TYR119 3.7 31.4 1.0 OH A:TYR119 4.0 31.6 1.0 C18 A:5QV503 4.1 23.6 1.0 C8 A:5QV503 4.1 24.6 1.0 N11 A:5QV503 4.3 24.0 1.0 CE1 A:TYR119 4.3 31.3 1.0 CZ A:PHE156 4.4 20.3 1.0 CG A:TYR119 4.4 31.5 1.0 CG A:PHE156 4.5 20.5 1.0 O A:HOH794 4.5 29.4 1.0 CD1 A:TYR119 4.7 31.4 1.0 F23 A:5QV503 4.7 23.7 1.0 C3 A:5QV503 5.0 25.0 1.0

Fluorine binding site 2 out of 2 in the Compound 18


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Compound 18 within 5.0Å range: probe atom residue distance (Å) B Occ A:F503 b:23.7 occ:1.00 F23 A:5QV503 0.0 23.7 1.0 C19 A:5QV503 1.3 23.7 1.0 C20 A:5QV503 2.4 23.4 1.0 C18 A:5QV503 2.4 23.6 1.0 O A:HOH823 2.7 0.0 1.0 C24 A:5QV503 2.9 23.6 1.0 C25 A:5QV503 3.0 23.8 1.0 O A:PHE156 3.4 20.5 1.0 CZ2 A:TRP163 3.6 19.2 1.0 C21 A:5QV503 3.6 23.5 1.0 C17 A:5QV503 3.6 23.6 1.0 CD1 A:ILE158 3.7 20.5 1.0 CH2 A:TRP163 3.8 19.2 1.0 CG1 A:ILE158 3.9 20.6 1.0 O A:HOH794 4.0 29.4 1.0 C29 A:5QV503 4.0 23.6 1.0 N26 A:5QV503 4.1 23.9 1.0 C16 A:5QV503 4.1 23.6 1.0 C A:PHE156 4.7 20.6 1.0 F22 A:5QV503 4.7 23.4 1.0 N28 A:5QV503 4.9 23.7 1.0 CE2 A:TRP163 4.9 19.0 1.0 C27 A:5QV503 5.0 23.9 1.0

Y.J.Wu, J.Guernon, F.Yang, L.Snyder, J.Shi, A.Mcclure, R.Rajamani, H.Park, A.Ng, H.Lewis, C.Chang, D.Camac, J.H.Toyn, M.K.Ahlijanian, C.F.Albright, J.E.Macor, L.A.Thompson. Targeting the BACE1 Active Site Flap Leads to A Potent Inhibitor That Elicits Robust Brain A Beta Reduction in Rodents. Acs Med.Chem.Lett. V. 7 271 2016.
ISSN: ISSN 1948-5875
PubMed: 26985314
DOI: 10.1021/ACSMEDCHEMLETT.5B00432