Fluorine in PDB 7d9o: Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2

All present enzymatic activity of Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2:
3.1.1.7;

The structure of Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2, PDB code: 7d9o was solved by Q.F.Liu, W.C.Yin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.89 / 2.45
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	104.866, 104.866, 324.416, 90, 90, 120
R / Rfree (%)	18.7 / 21.4

The binding sites of Fluorine atom in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2 (pdb code 7d9o). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2, PDB code: 7d9o:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2


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 Recombinant Human Acetylcholinesterase in Complex with Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:46.2 occ:1.00 F1 A:H0L601 0.0 46.2 1.0 C12 A:H0L601 1.4 33.7 1.0 C11 A:H0L601 2.3 33.1 1.0 C13 A:H0L601 2.3 38.8 1.0 C23 A:H0L601 2.4 34.7 1.0 C14 A:H0L601 2.7 37.2 1.0 C22 A:H0L601 2.8 36.6 1.0 CE2 A:PHE338 3.2 33.3 1.0 N1 A:H0L601 3.3 44.0 1.0 CZ A:PHE338 3.7 28.8 1.0 C10 A:H0L601 3.7 33.2 1.0 CD2 A:PHE338 4.0 33.0 1.0 C15 A:H0L601 4.3 42.3 1.0 C16 A:H0L601 4.4 39.0 1.0 C24 A:H0L601 4.5 28.0 1.0 CE1 A:PHE297 4.5 22.5 1.0 CZ A:PHE297 4.6 22.3 1.0 OH A:TYR124 4.6 32.9 1.0 C9 A:H0L601 4.7 30.3 1.0 C21 A:H0L601 4.7 39.2 1.0 C17 A:H0L601 4.8 37.9 1.0 CE1 A:PHE338 4.8 30.3 1.0 O3 A:H0L601 4.8 31.2 1.0

Fluorine binding site 2 out of 4 in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2


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 Recombinant Human Acetylcholinesterase in Complex with Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:47.4 occ:1.00 F2 A:H0L601 0.0 47.4 1.0 C19 A:H0L601 1.4 45.0 1.0 C18 A:H0L601 2.3 34.2 1.0 C20 A:H0L601 2.3 37.7 1.0 OE2 A:GLU202 3.1 34.9 1.0 O A:HOH751 3.2 29.9 1.0 C17 A:H0L601 3.6 37.9 1.0 C21 A:H0L601 3.6 39.2 1.0 C A:GLY120 3.7 26.4 1.0 N A:GLY121 3.8 31.1 1.0 CA A:GLY120 3.8 21.4 1.0 OH A:TYR133 4.0 32.2 1.0 C16 A:H0L601 4.1 39.0 1.0 O A:GLY120 4.1 32.0 1.0 CD A:GLU202 4.2 41.0 1.0 N A:GLY120 4.2 26.9 1.0 CB A:SER203 4.2 30.4 1.0 O A:HOH725 4.3 26.8 1.0 CZ3 A:TRP86 4.3 29.8 1.0 OG A:SER203 4.4 44.4 1.0 CA A:GLY121 4.5 21.8 1.0 CE3 A:TRP86 4.6 33.4 1.0 OE1 A:GLU202 4.7 39.8 1.0 CD1 A:ILE451 4.8 24.4 1.0 O A:GLU202 4.8 25.9 1.0 CH2 A:TRP86 4.9 37.5 1.0

Fluorine binding site 3 out of 4 in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:F601 b:41.6 occ:1.00 F1 B:H0L601 0.0 41.6 1.0 C12 B:H0L601 1.4 42.7 1.0 C11 B:H0L601 2.3 40.0 1.0 C13 B:H0L601 2.4 42.0 1.0 C23 B:H0L601 2.4 47.3 1.0 N1 B:H0L601 2.8 46.5 1.0 C14 B:H0L601 2.8 44.0 1.0 CE1 B:PHE338 3.1 32.5 1.0 C22 B:H0L601 3.1 36.5 1.0 CZ B:PHE338 3.6 33.8 1.0 C10 B:H0L601 3.7 38.6 1.0 CD1 B:PHE338 3.9 35.6 1.0 C15 B:H0L601 4.1 48.0 1.0 C16 B:H0L601 4.4 47.5 1.0 C24 B:H0L601 4.6 31.6 1.0 CZ B:PHE297 4.6 29.2 1.0 CE1 B:PHE297 4.6 27.5 1.0 OH B:TYR124 4.7 37.0 1.0 C21 B:H0L601 4.7 42.8 1.0 C9 B:H0L601 4.8 37.8 1.0 CE2 B:PHE338 4.8 31.4 1.0 C17 B:H0L601 4.9 38.5 1.0 O3 B:H0L601 4.9 39.3 1.0

Fluorine binding site 4 out of 4 in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:F601 b:56.7 occ:1.00 F2 B:H0L601 0.0 56.7 1.0 C19 B:H0L601 1.4 53.0 1.0 C20 B:H0L601 2.3 41.0 1.0 C18 B:H0L601 2.4 40.6 1.0 O B:HOH755 2.9 31.1 1.0 OE2 B:GLU202 2.9 43.2 1.0 N B:GLY121 3.5 26.1 1.0 C21 B:H0L601 3.6 42.8 1.0 C17 B:H0L601 3.6 38.5 1.0 C B:GLY120 3.6 31.6 1.0 CA B:GLY120 3.7 24.5 1.0 OH B:TYR133 3.8 30.6 1.0 N B:GLY120 4.1 22.4 1.0 C16 B:H0L601 4.1 47.5 1.0 CD B:GLU202 4.1 46.8 1.0 CZ3 B:TRP86 4.2 33.4 1.0 CB B:SER203 4.2 35.9 1.0 O B:GLY120 4.2 33.2 1.0 O B:HOH750 4.3 26.7 1.0 CA B:GLY121 4.4 25.3 1.0 O B:GLU202 4.4 30.8 1.0 CE3 B:TRP86 4.5 35.0 1.0 CD1 B:ILE451 4.6 30.9 1.0 OE1 B:GLU202 4.7 42.2 1.0 OG B:SER203 4.7 35.3 1.0 CH2 B:TRP86 4.8 33.4 1.0 C B:GLU202 5.0 31.0 1.0

Y.Zhou, Y.Fu, W.Yin, J.Li, W.Wang, F.Bai, S.Xu, Q.Gong, T.Peng, Y.Hong, D.Zhang, D.Zhang, Q.Liu, Y.Xu, H.E.Xu, H.Zhang, H.Jiang, H.Liu. Kinetics-Driven Drug Design Strategy For Next-Generation Acetylcholinesterase Inhibitors to Clinical Candidate. J.Med.Chem. V. 64 1844 2021.
ISSN: ISSN 0022-2623
PubMed: 33570950
DOI: 10.1021/ACS.JMEDCHEM.0C01863