Bromine in PDB 2whr: Crystal Structure of Acetylcholinesterase in Complex with K027

All present enzymatic activity of Crystal Structure of Acetylcholinesterase in Complex with K027:
3.1.1.7;

The structure of Crystal Structure of Acetylcholinesterase in Complex with K027, PDB code: 2whr was solved by F.Ekstrom, A.Hornberg, E.Artursson, L.-G.Hammarstrom, G.Schneider, Y.-P.Pang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.81 / 2.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	78.320, 111.410, 226.850, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 21.9

The binding sites of Bromine atom in the Crystal Structure of Acetylcholinesterase in Complex with K027 (pdb code 2whr). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of Acetylcholinesterase in Complex with K027, PDB code: 2whr:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Acetylcholinesterase in Complex with K027


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Acetylcholinesterase in Complex with K027 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1546 b:38.3 occ:1.00 O A:HOH2277 3.2 39.5 1.0 N A:PHE295 3.3 32.7 1.0 C9 A:K271543 3.6 29.3 1.0 C5 A:K271543 3.6 37.4 1.0 C2 A:K271543 3.6 31.5 1.0 O A:HOH2253 3.7 40.5 1.0 CD2 A:PHE338 3.8 32.5 1.0 CA A:ILE294 3.9 33.2 1.0 C1 A:K271543 4.0 34.0 1.0 C A:ILE294 4.1 29.4 1.0 CB A:ILE294 4.1 29.0 1.0 N8 A:K271543 4.1 32.6 1.0 CA A:PHE295 4.2 26.1 1.0 C3 A:K271543 4.2 42.9 1.0 CB A:TYR341 4.4 34.0 1.0 CG2 A:ILE294 4.4 22.9 1.0 CE2 A:PHE338 4.4 26.4 1.0 N2 A:K271543 4.6 42.0 1.0 CE1 A:PHE297 4.7 28.1 1.0 C10 A:K271543 4.7 34.0 1.0 N A:ARG296 4.7 28.1 1.0 O A:HOH2245 4.8 37.6 1.0 CG A:PHE338 4.9 32.5 1.0 CB A:PHE338 4.9 32.3 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of Acetylcholinesterase in Complex with K027


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Acetylcholinesterase in Complex with K027 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br1546 b:46.4 occ:1.00 O B:HOH2194 3.2 29.0 0.5 N B:PHE295 3.3 34.5 1.0 C5 B:K271545 3.7 38.1 1.0 O B:HOH2177 3.7 27.8 0.5 C9 B:K271545 3.8 42.3 1.0 CD2 B:PHE338 3.8 31.7 1.0 CA B:ILE294 3.9 35.1 1.0 C2 B:K271545 3.9 41.5 1.0 C1 B:K271545 3.9 42.7 1.0 C B:ILE294 4.1 36.9 1.0 CA B:PHE295 4.1 30.3 1.0 C3 B:K271545 4.1 56.3 1.0 CB B:ILE294 4.1 35.9 1.0 N8 B:K271545 4.3 44.6 1.0 CB B:TYR341 4.4 36.7 1.0 CG2 B:ILE294 4.4 36.9 1.0 CE2 B:PHE338 4.5 35.9 1.0 O B:HOH2170 4.5 26.3 0.5 CE1 B:PHE297 4.5 35.2 1.0 N2 B:K271545 4.5 56.1 1.0 N B:ARG296 4.6 33.1 1.0 CG B:PHE338 4.8 38.4 1.0 CB B:PHE338 4.9 35.3 1.0 O B:PHE338 4.9 36.8 1.0 C10 B:K271545 4.9 39.6 1.0 C B:PHE295 5.0 34.2 1.0

F.Ekstrom, A.Hornberg, E.Artursson, L.-G.Hammarstrom, G.Schneider, Y.-P.Pang. Structure of Hi-6SARIN-Acetylcholinesterase Determined By X-Ray Crystallography and Molecular Dynamics Simulation: Reactivator Mechanism and Design. Plos One V. 4 E5957 2009.
ISSN: ESSN 1932-6203
PubMed: 19536291
DOI: 10.1371/JOURNAL.PONE.0005957