Fluorine in PDB 5enm: Compound 10

All present enzymatic activity of Compound 10:
3.4.23.46;

The structure of Compound 10, PDB code: 5enm 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 / 1.98
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.234, 102.234, 170.579, 90.00, 90.00, 120.00
R / Rfree (%)	25.5 / 28.4

The structure of Compound 10 also contains other interesting chemical elements:

Iodine

(I)

1 atom

The binding sites of Fluorine atom in the Compound 10 (pdb code 5enm). 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 10, PDB code: 5enm:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Compound 10


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Compound 10 within 5.0Å range: probe atom residue distance (Å) B Occ A:F503 b:31.9 occ:1.00 F21 A:5QU503 0.0 31.9 1.0 C20 A:5QU503 1.3 31.7 1.0 C19 A:5QU503 2.3 31.7 1.0 C15 A:5QU503 2.4 31.7 1.0 C10 A:5QU503 3.0 31.9 1.0 CE1 A:PHE156 3.1 31.1 1.0 CD1 A:PHE156 3.2 31.1 1.0 C9 A:5QU503 3.3 32.0 1.0 OH A:TYR119 3.4 44.3 1.0 CZ A:TYR119 3.5 44.1 1.0 CE2 A:TYR119 3.5 44.1 1.0 C18 A:5QU503 3.6 31.8 1.0 C16 A:5QU503 3.7 31.4 1.0 CD1 A:ILE166 4.0 24.3 1.0 C17 A:5QU503 4.1 31.7 1.0 CE1 A:TYR119 4.2 44.3 1.0 CD2 A:TYR119 4.2 44.1 1.0 CZ A:PHE156 4.3 31.1 1.0 N11 A:5QU503 4.4 31.9 1.0 C8 A:5QU503 4.5 32.5 1.0 CG A:PHE156 4.5 31.3 1.0 F22 A:5QU503 4.7 32.0 1.0 CD1 A:TYR119 4.9 44.3 1.0 CG A:TYR119 4.9 44.0 1.0

Fluorine binding site 2 out of 2 in the Compound 10


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Compound 10 within 5.0Å range: probe atom residue distance (Å) B Occ A:F503 b:32.0 occ:1.00 F22 A:5QU503 0.0 32.0 1.0 C18 A:5QU503 1.3 31.8 1.0 C19 A:5QU503 2.4 31.7 1.0 C17 A:5QU503 2.4 31.7 1.0 O A:HOH603 2.6 35.9 1.0 C23 A:5QU503 2.9 31.7 1.0 C24 A:5QU503 3.0 31.9 1.0 CZ2 A:TRP163 3.2 27.6 1.0 CH2 A:TRP163 3.4 27.4 1.0 O A:PHE156 3.5 31.4 1.0 C16 A:5QU503 3.6 31.4 1.0 C20 A:5QU503 3.6 31.7 1.0 CD1 A:ILE158 3.7 32.0 1.0 CG1 A:ILE158 3.9 31.9 1.0 C28 A:5QU503 4.0 31.7 1.0 N25 A:5QU503 4.1 31.9 1.0 C15 A:5QU503 4.2 31.7 1.0 CE2 A:TRP163 4.5 27.5 1.0 CD2 A:LEU78 4.6 23.9 1.0 C A:PHE156 4.7 31.5 1.0 F21 A:5QU503 4.7 31.9 1.0 CZ3 A:TRP163 4.7 27.4 1.0 N27 A:5QU503 4.9 31.5 1.0 C26 A:5QU503 5.0 31.8 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