Chlorine in PDB 4bds: Human Butyrylcholinesterase in Complex with Tacrine

All present enzymatic activity of Human Butyrylcholinesterase in Complex with Tacrine:
3.1.1.8;

The structure of Human Butyrylcholinesterase in Complex with Tacrine, PDB code: 4bds was solved by F.Nachon, E.Carletti, C.Ronco, M.Trovaslet, Y.Nicolet, L.Jean, P.-Y.Renard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.90 / 2.10
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	155.660, 155.660, 127.880, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 20.9

The binding sites of Chlorine atom in the Human Butyrylcholinesterase in Complex with Tacrine (pdb code 4bds). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Butyrylcholinesterase in Complex with Tacrine, PDB code: 4bds:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Butyrylcholinesterase in Complex with Tacrine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Butyrylcholinesterase in Complex with Tacrine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl705 b:60.4 occ:1.00 O A:HOH2240 3.1 38.0 1.0 CG2 A:THR508 3.2 50.0 1.0 N A:THR488 3.5 46.7 1.0 OG1 A:THR508 3.6 51.8 1.0 OG1 A:THR488 3.7 52.0 1.0 CA A:SER487 3.9 49.9 1.0 CB A:THR508 4.0 49.7 1.0 C A:SER487 4.2 50.0 1.0 CB A:THR488 4.3 44.7 1.0 CB A:SER487 4.4 47.8 1.0 CA A:THR488 4.5 42.5 1.0 OG A:SER487 4.5 52.2 1.0 O A:GLN486 4.6 63.3 1.0 N A:THR508 5.0 43.8 1.0

Chlorine binding site 2 out of 2 in the Human Butyrylcholinesterase in Complex with Tacrine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Butyrylcholinesterase in Complex with Tacrine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl706 b:63.1 occ:1.00 O A:HOH2271 2.5 55.9 1.0 OH A:TYR420 3.2 28.1 1.0 CE A:LYS323 3.8 51.6 1.0 NH1 A:ARG515 4.1 38.2 1.0 CG A:LYS323 4.2 33.3 1.0 CZ A:TYR420 4.2 28.4 1.0 CD A:LYS323 4.3 44.0 1.0 O A:HOH2270 4.3 40.4 1.0 CE2 A:TYR420 4.3 29.8 1.0 O A:HOH2165 4.4 38.9 1.0 NZ A:LYS323 4.6 64.0 1.0 NH2 A:ARG515 4.7 31.1 1.0 CZ A:ARG515 4.7 43.5 1.0

F.Nachon, E.Carletti, C.Ronco, M.Trovaslet, Y.Nicolet, L.Jean, P.Renard. Crystal Structures of Human Cholinesterases in Complex with Huprine W and Tacrine: Elements of Specificity For Anti-Alzheimer'S Drugs Targeting Acetyl- and Butyrylcholinesterase. Biochem.J. V. 453 393 2013.
ISSN: ISSN 0264-6021
PubMed: 23679855
DOI: 10.1042/BJ20130013