Fluorine in PDB 1amn: Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone

All present enzymatic activity of Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone:
3.1.1.7;

The structure of Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone, PDB code: 1amn was solved by M.Harel, I.Silman, J.L.Sussman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.80
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	113.540, 113.540, 137.530, 90.00, 90.00, 120.00
R / Rfree (%)	18.8 / 23.5

The binding sites of Fluorine atom in the Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone (pdb code 1amn). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone, PDB code: 1amn:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone within 5.0Å range: probe atom residue distance (Å) B Occ A:F594 b:10.8 occ:1.00 F1' A:NAF594 0.0 10.8 1.0 C2' A:NAF594 1.4 7.3 1.0 F3' A:NAF594 2.2 17.9 1.0 F2' A:NAF594 2.4 13.0 1.0 C1' A:NAF594 2.5 12.2 1.0 O1' A:NAF594 2.8 4.6 1.0 C4 A:NAF594 2.8 11.0 1.0 H A:GLY119 2.8 15.0 1.0 C3 A:NAF594 3.0 13.9 1.0 CA A:GLY119 3.2 2.0 1.0 N A:GLY119 3.2 2.0 1.0 CZ A:PHE290 3.3 17.4 1.0 CE2 A:PHE290 3.4 12.0 1.0 O2' A:NAF594 3.8 15.2 1.0 CE1 A:PHE288 3.8 14.3 1.0 C5 A:NAF594 4.0 12.3 1.0 CZ3 A:TRP233 4.4 2.0 1.0 CE1 A:PHE290 4.4 16.7 1.0 CZ A:PHE288 4.4 10.9 1.0 C A:GLY118 4.4 9.2 1.0 CD2 A:PHE290 4.4 8.9 1.0 H A:GLY118 4.5 15.0 1.0 C2 A:NAF594 4.5 14.7 1.0 CE3 A:TRP233 4.5 2.8 1.0 C A:GLY119 4.6 9.3 1.0 CH2 A:TRP233 4.6 2.0 1.0 HE2 A:HIS440 4.6 15.0 1.0 CB A:SER200 4.6 13.2 1.0 CE1 A:PHE331 4.7 10.0 1.0 CD1 A:PHE288 4.7 8.5 1.0 CD2 A:TRP233 4.8 4.8 1.0 CZ A:PHE331 4.8 12.2 1.0 H A:ALA201 4.8 15.0 1.0 CZ2 A:TRP233 4.9 2.0 1.0 N A:ALA201 5.0 7.2 1.0 CE2 A:TRP233 5.0 8.5 1.0

Fluorine binding site 2 out of 3 in the Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone within 5.0Å range: probe atom residue distance (Å) B Occ A:F594 b:13.0 occ:1.00 F2' A:NAF594 0.0 13.0 1.0 C2' A:NAF594 1.4 7.3 1.0 F3' A:NAF594 2.3 17.9 1.0 F1' A:NAF594 2.4 10.8 1.0 C1' A:NAF594 2.4 12.2 1.0 O2' A:NAF594 2.9 15.2 1.0 CZ A:PHE288 2.9 10.9 1.0 HE2 A:HIS440 3.0 15.0 1.0 C3 A:NAF594 3.1 13.9 1.0 CE1 A:PHE288 3.2 14.3 1.0 C4 A:NAF594 3.4 11.0 1.0 NE2 A:HIS440 3.4 7.0 1.0 CE1 A:HIS440 3.4 4.4 1.0 CZ A:PHE331 3.4 12.2 1.0 O1' A:NAF594 3.5 4.6 1.0 CE1 A:PHE331 3.9 10.0 1.0 CB A:SER200 4.1 13.2 1.0 CE2 A:PHE288 4.1 7.7 1.0 CE2 A:PHE331 4.3 9.9 1.0 C2 A:NAF594 4.3 14.7 1.0 CD1 A:PHE288 4.4 8.5 1.0 CD2 A:HIS440 4.5 8.8 1.0 ND1 A:HIS440 4.5 3.8 1.0 CZ2 A:TRP233 4.6 2.0 1.0 C5 A:NAF594 4.6 12.3 1.0 H A:GLY119 4.7 15.0 1.0 CA A:SER200 4.8 8.8 1.0 CH2 A:TRP233 4.8 2.0 1.0 CE2 A:TRP233 4.8 8.5 1.0 CZ A:PHE290 4.9 17.4 1.0 HD1 A:HIS440 4.9 15.0 1.0

Fluorine binding site 3 out of 3 in the Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Transition State Analog: Acetylcholinesterase Complexed with M-(N,N,N-Trimethylammonio)Trifluoroacetophenone within 5.0Å range: probe atom residue distance (Å) B Occ A:F594 b:17.9 occ:1.00 F3' A:NAF594 0.0 17.9 1.0 C2' A:NAF594 1.4 7.3 1.0 F1' A:NAF594 2.2 10.8 1.0 F2' A:NAF594 2.3 13.0 1.0 C1' A:NAF594 2.5 12.2 1.0 CH2 A:TRP233 2.8 2.0 1.0 O1' A:NAF594 2.9 4.6 1.0 O2' A:NAF594 2.9 15.2 1.0 CZ2 A:TRP233 3.2 2.0 1.0 CZ3 A:TRP233 3.2 2.0 1.0 CB A:SER200 3.5 13.2 1.0 C A:SER200 3.5 9.6 1.0 N A:ALA201 3.6 7.2 1.0 CA A:SER200 3.7 8.8 1.0 CE2 A:TRP233 3.8 8.5 1.0 H A:GLY119 3.8 15.0 1.0 H A:ALA201 3.8 15.0 1.0 C3 A:NAF594 3.8 13.9 1.0 CE3 A:TRP233 3.9 2.8 1.0 O A:SER200 4.0 16.4 1.0 CD2 A:TRP233 4.1 4.8 1.0 CE1 A:PHE288 4.1 14.3 1.0 CA A:ALA201 4.2 9.2 1.0 HE2 A:HIS440 4.3 15.0 1.0 C4 A:NAF594 4.3 11.0 1.0 CZ A:PHE288 4.4 10.9 1.0 CB A:ALA201 4.5 7.5 1.0 N A:GLY119 4.6 2.0 1.0 CA A:GLY119 4.6 2.0 1.0 CE1 A:HIS440 4.7 4.4 1.0 H A:GLY118 4.8 15.0 1.0 NE1 A:TRP233 4.8 6.5 1.0 NE2 A:HIS440 4.8 7.0 1.0 CE2 A:PHE290 4.9 12.0 1.0 O A:SER226 4.9 9.4 1.0

M.Harel, D.M.Quinn, H.K.Nair, I.Silman, J.L.Sussman. The X-Ray Structure of A Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase. J.Am.Chem.Soc. V. 118 2340 1996.
ISSN: ISSN 0002-7863