Chlorine in PDB 3dkk: Aged Form of Human Butyrylcholinesterase Inhibited By Tabun

All present enzymatic activity of Aged Form of Human Butyrylcholinesterase Inhibited By Tabun:
3.1.1.8;

The structure of Aged Form of Human Butyrylcholinesterase Inhibited By Tabun, PDB code: 3dkk was solved by F.Nachon, E.Carletti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.18 / 2.31
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	155.240, 155.240, 127.470, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 25.1

The structure of Aged Form of Human Butyrylcholinesterase Inhibited By Tabun also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Aged Form of Human Butyrylcholinesterase Inhibited By Tabun (pdb code 3dkk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Aged Form of Human Butyrylcholinesterase Inhibited By Tabun, PDB code: 3dkk:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Aged Form of Human Butyrylcholinesterase Inhibited By Tabun


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Aged Form of Human Butyrylcholinesterase Inhibited By Tabun within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl541 b:63.6 occ:1.00 NH1 A:ARG347 4.0 54.1 1.0 NE A:ARG347 4.1 53.2 1.0 NE2 A:GLN351 4.2 44.5 1.0 CZ A:ARG347 4.6 53.3 1.0 OE1 A:GLN351 4.6 44.0 1.0 CD A:GLN351 4.9 42.6 1.0

Chlorine binding site 2 out of 2 in the Aged Form of Human Butyrylcholinesterase Inhibited By Tabun


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Aged Form of Human Butyrylcholinesterase Inhibited By Tabun within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl542 b:57.6 occ:1.00 OG1 A:THR508 3.7 44.2 1.0 N A:THR488 3.8 48.1 1.0 OG1 A:THR488 4.0 47.0 1.0 CA A:SER487 4.1 51.1 1.0 OG A:SER487 4.4 51.9 1.0 CB A:SER487 4.4 50.9 1.0 C A:SER487 4.4 49.7 1.0 CB A:THR488 4.6 45.9 1.0 CG2 A:THR508 4.6 46.5 1.0 CB A:THR508 4.6 45.8 1.0 N A:THR508 4.7 47.1 1.0 O A:GLN486 4.7 53.6 1.0 CA A:THR488 4.8 46.2 1.0

E.Carletti, H.Li, B.Li, F.Ekstrom, Y.Nicolet, M.Loiodice, E.Gillon, M.T.Froment, O.Lockridge, L.M.Schopfer, P.Masson, F.Nachon. Aging of Cholinesterases Phosphylated By Tabun Proceeds Through O-Dealkylation. J.Am.Chem.Soc. V. 130 16011 2008.
ISSN: ISSN 0002-7863
PubMed: 18975951
DOI: 10.1021/JA804941Z