Fluorine in PDB 7d9q: Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 7

All present enzymatic activity of Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 7:
3.1.1.7;

The structure of Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 7, PDB code: 7d9q 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)	49.80 / 2.66
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	104.649, 104.649, 324.403, 90, 90, 120
R / Rfree (%)	18.3 / 21.9

The binding sites of Fluorine atom in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 7 (pdb code 7d9q). 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 7, PDB code: 7d9q:
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 7


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 7 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:48.2 occ:1.00 F16 A:H1R601 0.0 48.2 1.0 C15 A:H1R601 1.4 41.7 1.0 C29 A:H1R601 2.3 39.6 1.0 C17 A:H1R601 2.4 31.2 1.0 C14 A:H1R601 2.4 37.0 1.0 C13 A:H1R601 2.8 34.7 1.0 C28 A:H1R601 3.1 42.6 1.0 CE2 A:PHE338 3.3 37.0 1.0 N19 A:H1R601 3.4 58.5 1.0 C18 A:H1R601 3.5 33.8 1.0 CD2 A:PHE338 3.8 39.5 1.0 C11 A:H1R601 3.8 36.0 1.0 O12 A:H1R601 4.0 41.3 1.0 C30 A:H1R601 4.0 28.9 1.0 CZ A:PHE338 4.1 37.6 1.0 CE1 A:PHE297 4.2 34.8 1.0 CZ A:PHE297 4.3 31.8 1.0 OH A:TYR124 4.4 41.3 1.0 C20 A:H1R601 4.6 52.1 1.0 CG A:PHE338 4.9 42.9 1.0 CE2 A:TYR124 5.0 31.7 1.0

Fluorine binding site 2 out of 4 in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 7


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 7 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:51.9 occ:1.00 F26 A:H1R601 0.0 51.9 1.0 C25 A:H1R601 1.4 46.6 1.0 C24 A:H1R601 2.4 42.3 1.0 C27 A:H1R601 2.4 44.0 1.0 N A:GLY121 3.5 34.7 1.0 C A:GLY120 3.5 33.8 1.0 O A:GLY120 3.6 36.2 1.0 CA A:GLY121 3.6 22.8 1.0 C23 A:H1R601 3.6 48.2 1.0 C21 A:H1R601 3.6 48.5 1.0 CE3 A:TRP86 4.0 35.1 1.0 OH A:TYR133 4.0 32.0 1.0 C22 A:H1R601 4.1 51.9 1.0 CZ3 A:TRP86 4.2 37.6 1.0 CA A:GLY120 4.2 35.0 1.0 OE2 A:GLU202 4.4 50.0 1.0 CD2 A:TRP86 4.7 44.1 1.0 N A:GLY120 4.7 37.2 1.0 C20 A:H1R601 4.9 52.1 1.0 C A:GLY121 5.0 25.4 1.0

Fluorine binding site 3 out of 4 in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 7


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 7 within 5.0Å range: probe atom residue distance (Å) B Occ B:F601 b:42.4 occ:1.00 F16 B:H1R601 0.0 42.4 1.0 C15 B:H1R601 1.4 46.2 1.0 C29 B:H1R601 2.3 50.6 1.0 C17 B:H1R601 2.4 47.9 1.0 C14 B:H1R601 2.4 43.4 1.0 C13 B:H1R601 2.9 34.9 1.0 C28 B:H1R601 3.2 49.9 1.0 CE1 B:PHE338 3.2 30.3 1.0 N19 B:H1R601 3.2 62.9 1.0 C18 B:H1R601 3.3 49.0 1.0 CD1 B:PHE338 3.8 38.5 1.0 C30 B:H1R601 4.0 35.4 1.0 C11 B:H1R601 4.0 43.0 1.0 OH B:TYR124 4.0 36.2 1.0 CZ B:PHE338 4.1 39.4 1.0 CE1 B:PHE297 4.2 30.2 1.0 O12 B:H1R601 4.2 39.8 1.0 C20 B:H1R601 4.4 63.4 1.0 CZ B:PHE297 4.5 29.5 1.0 CE2 B:TYR124 4.8 41.0 1.0 C21 B:H1R601 4.9 61.7 1.0 CZ B:TYR124 4.9 34.6 1.0

Fluorine binding site 4 out of 4 in the Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with Compound 7


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 7 within 5.0Å range: probe atom residue distance (Å) B Occ B:F601 b:60.2 occ:1.00 F26 B:H1R601 0.0 60.2 1.0 C25 B:H1R601 1.4 48.9 1.0 C27 B:H1R601 2.4 41.1 1.0 C24 B:H1R601 2.4 50.7 1.0 N B:GLY121 3.2 34.7 1.0 C B:GLY120 3.3 34.5 1.0 CA B:GLY121 3.5 22.2 1.0 O B:GLY120 3.5 40.3 1.0 C21 B:H1R601 3.6 61.7 1.0 C23 B:H1R601 3.7 44.0 1.0 OH B:TYR133 3.8 34.3 1.0 CE3 B:TRP86 4.0 33.8 1.0 CA B:GLY120 4.0 29.3 1.0 C22 B:H1R601 4.1 49.4 1.0 CZ3 B:TRP86 4.3 42.1 1.0 OE2 B:GLU202 4.4 55.5 1.0 N B:GLY120 4.5 29.0 1.0 CD2 B:TRP86 4.7 38.9 1.0 C20 B:H1R601 4.9 63.4 1.0 C B:GLY121 5.0 35.4 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