Fluorine in PDB 4b82: Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide

All present enzymatic activity of Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide:
3.1.1.7;

The structure of Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide, PDB code: 4b82 was solved by C.D.Andersson, N.Forsgren, C.Akfur, A.Allgardsson, L.Berg, W.Qian, F.J.Ekstrom, A.Linusson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.810 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	80.460, 111.858, 226.930, 90.00, 90.00, 90.00
R / Rfree (%)	19.09 / 21.52

The binding sites of Fluorine atom in the Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide (pdb code 4b82). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide, PDB code: 4b82:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:F1543 b:43.9 occ:0.72 F09 A:B3Z1543 0.0 43.9 0.7 C10 A:B3Z1543 1.3 43.7 0.7 C6 A:B3Z1543 1.3 43.5 0.3 C5 A:B3Z1543 2.2 43.4 0.3 C9 A:B3Z1543 2.3 42.8 0.7 C5 A:B3Z1543 2.3 43.3 0.7 C7 A:B3Z1543 2.3 42.9 0.3 N4 A:B3Z1543 2.4 41.5 0.3 N4 A:B3Z1543 2.4 41.2 0.7 S1 A:B3Z1543 2.8 46.8 0.3 S1 A:B3Z1543 2.9 46.7 0.7 OH A:TYR124 2.9 35.4 1.0 O A:HOH2386 3.0 33.7 1.0 O A:HOH2122 3.2 44.5 1.0 O2 A:B3Z1543 3.2 48.2 0.3 O2 A:B3Z1543 3.3 49.1 0.7 C10 A:B3Z1543 3.4 43.4 0.3 C6 A:B3Z1543 3.5 43.7 0.7 C8 A:B3Z1543 3.5 42.9 0.3 C8 A:B3Z1543 3.6 42.6 0.7 C22 A:B3Z1543 3.7 42.1 0.7 C22 A:B3Z1543 3.8 41.5 0.3 C9 A:B3Z1543 4.0 43.2 0.3 O A:HOH2199 4.0 30.1 1.0 C7 A:B3Z1543 4.0 43.3 0.7 O A:HOH2144 4.0 35.1 1.0 O1 A:B3Z1543 4.1 45.4 0.3 CZ A:TYR124 4.2 32.9 1.0 O1 A:B3Z1543 4.2 44.3 0.7 OD2 A:ASP74 4.2 43.4 1.0 O A:HOH2127 4.4 35.3 1.0 F09 A:B3Z1543 4.5 42.5 0.3 CE1 A:TYR337 4.5 29.4 1.0 OH A:TYR341 4.7 33.0 1.0 C21 A:B3Z1543 4.7 38.1 0.7 C21 A:B3Z1543 4.7 36.9 0.3 OH A:TYR337 4.8 27.6 1.0 CZ A:TYR341 4.8 34.6 1.0 CE1 A:TYR124 4.9 33.7 1.0 CG A:ASP74 5.0 41.8 1.0

Fluorine binding site 2 out of 3 in the Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:F1543 b:42.5 occ:0.28 F09 A:B3Z1543 0.0 42.5 0.3 C10 A:B3Z1543 1.3 43.4 0.3 C6 A:B3Z1543 1.3 43.7 0.7 C5 A:B3Z1543 2.2 43.3 0.7 C9 A:B3Z1543 2.3 43.2 0.3 C5 A:B3Z1543 2.3 43.4 0.3 C7 A:B3Z1543 2.4 43.3 0.7 CE2 A:PHE338 2.9 35.5 1.0 S1 A:B3Z1543 3.0 46.7 0.7 O1 A:B3Z1543 3.0 44.3 0.7 S1 A:B3Z1543 3.1 46.8 0.3 O1 A:B3Z1543 3.1 45.4 0.3 CE1 A:PHE297 3.3 26.3 1.0 O2 A:B3Z1543 3.4 49.1 0.7 C10 A:B3Z1543 3.5 43.7 0.7 CZ A:PHE297 3.5 26.2 1.0 O2 A:B3Z1543 3.6 48.2 0.3 C6 A:B3Z1543 3.6 43.5 0.3 C8 A:B3Z1543 3.6 42.9 0.3 C8 A:B3Z1543 3.6 42.6 0.7 CD2 A:PHE338 3.6 33.2 1.0 CZ A:PHE338 3.7 32.5 1.0 C9 A:B3Z1543 4.0 42.8 0.7 C7 A:B3Z1543 4.0 42.9 0.3 F09 A:B3Z1543 4.5 43.9 0.7 N4 A:B3Z1543 4.5 41.2 0.7 O A:HOH2359 4.5 36.4 1.0 CD1 A:PHE297 4.6 24.8 1.0 N4 A:B3Z1543 4.6 41.5 0.3 OH A:TYR124 4.7 35.4 1.0 CE1 A:TYR124 4.7 33.7 1.0 O A:HOH2192 4.7 32.0 1.0 O A:HOH2173 4.8 55.2 1.0 CE2 A:PHE297 4.9 26.4 1.0 CG A:PHE338 4.9 32.5 1.0 CE1 A:PHE338 4.9 32.5 1.0

Fluorine binding site 3 out of 3 in the Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Mus Musculus Acetylcholinesterase in Complex with N-(2-Diethylamino- Ethyl)-2-Fluoranyl-Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ B:F1544 b:61.3 occ:1.00 F09 B:B3Z1544 0.0 61.3 1.0 C10 B:B3Z1544 1.3 57.8 1.0 C9 B:B3Z1544 2.3 56.9 1.0 C5 B:B3Z1544 2.3 56.4 1.0 N4 B:B3Z1544 2.4 45.2 1.0 S1 B:B3Z1544 2.9 46.8 1.0 O B:HOH2280 2.9 40.0 1.0 OH B:TYR124 2.9 39.3 1.0 O B:HOH2084 3.2 44.4 1.0 O2 B:B3Z1544 3.4 46.6 1.0 C6 B:B3Z1544 3.5 57.2 1.0 C8 B:B3Z1544 3.6 57.8 1.0 C22 B:B3Z1544 3.7 48.1 1.0 O B:HOH2140 3.8 30.1 1.0 C7 B:B3Z1544 4.0 57.6 1.0 O B:HOH2108 4.0 41.8 1.0 O1 B:B3Z1544 4.2 43.6 1.0 CZ B:TYR124 4.2 36.9 1.0 O B:HOH2089 4.3 39.6 1.0 OD1 B:ASP74 4.3 49.8 1.0 CE1 B:TYR337 4.5 35.3 1.0 C21 B:B3Z1544 4.6 44.0 1.0 OH B:TYR341 4.7 43.4 1.0 OH B:TYR337 4.7 38.1 1.0 CZ B:TYR341 4.9 42.0 1.0 CE1 B:TYR124 4.9 37.3 1.0 CG B:ASP74 5.0 50.1 1.0

C.D.Andersson, N.Forsgren, C.Akfur, A.Allgardsson, L.Berg, C.Engdahl, W.Qian, F.J.Ekstrom, A.Linusson. Divergent Structure-Activity Relationships of Structurally Similar Acetylcholinesterase Inhibitors. J.Med.Chem. V. 56 7615 2013.
ISSN: ISSN 0022-2623
PubMed: 23984975
DOI: 10.1021/JM400990P