Chlorine in PDB 2xqf: X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx

All present enzymatic activity of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx:
3.1.1.8;

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx, PDB code: 2xqf was solved by M.Wandhammer, E.Carletti, E.Gillon, P.Masson, M.Goeldner, D.Noort, F.Nachon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.00 / 2.10
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	155.110, 155.110, 128.100, 90.00, 90.00, 90.00
R / Rfree (%)	14.9 / 18.9

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx also contains other interesting chemical elements:

Sodium	(Na)	1 atom
Potassium	(K)	1 atom

The binding sites of Chlorine atom in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx (pdb code 2xqf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx, PDB code: 2xqf:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1533 b:72.5 occ:1.00 NH1 A:ARG347 3.5 61.4 1.0 NE A:ARG347 3.5 53.8 1.0 NE2 A:GLN351 3.7 47.4 1.0 O A:HOH2271 3.9 42.2 1.0 CZ A:ARG347 3.9 56.4 1.0 CD A:ARG347 4.6 51.3 1.0 CD A:GLN351 4.7 46.3 1.0 OE1 A:GLN351 4.8 45.5 1.0

Chlorine binding site 2 out of 2 in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1534 b:69.5 occ:1.00 O A:HOH2388 3.0 22.8 1.0 OG1 A:THR512 3.1 32.4 1.0 O A:HOH2407 3.7 22.9 1.0 CB A:THR512 3.8 27.5 1.0 CE A:LYS513 4.1 40.5 1.0 CD A:LYS513 4.2 33.6 1.0 CG2 A:THR512 4.3 27.8 1.0 NZ A:LYS513 4.4 49.6 1.0 CG A:LYS513 4.6 29.2 1.0

M.Wandhammer, E.Carletti, M.Van Der Schans, E.Gillon, Y.Nicolet, P.Masson, M.Goeldner, D.Noort, F.Nachon. Structural Study of the Complex Stereoselectivity of Human Butyrylcholinesterase For the Neurotoxic V-Agents. J.Biol.Chem. V. 286 16783 2011.
ISSN: ISSN 0021-9258
PubMed: 21454498
DOI: 10.1074/JBC.M110.209569