Chlorine in PDB 2wif: Aged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1

All present enzymatic activity of Aged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1:
3.1.1.8;

The structure of Aged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1, PDB code: 2wif was solved by E.Carletti, N.Aurbek, E.Gillon, M.Loiodice, Y.Nicolet, J.Fontecilla, P.Masson, H.Thiermann, F.Nachon, F.Worek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.67 / 2.25
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	154.390, 154.390, 126.420, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 27.5

The structure of Aged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1 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 Analogue TA1 (pdb code 2wif). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Aged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1, PDB code: 2wif:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Aged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1


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 Analogue TA1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl602 b:58.8 occ:1.00 OG1 A:THR508 3.3 42.6 1.0 N A:THR488 3.5 43.6 1.0 O A:HOH932 3.8 47.2 1.0 OG1 A:THR488 3.8 44.0 1.0 CA A:SER487 3.9 48.7 1.0 CB A:THR488 4.2 41.2 1.0 C A:SER487 4.2 46.1 1.0 CB A:SER487 4.3 48.0 1.0 OG A:SER487 4.4 51.4 1.0 CA A:THR488 4.4 40.6 1.0 CB A:THR508 4.5 45.5 1.0 O A:ASN486 4.5 51.9 1.0 N A:THR508 4.6 46.7 1.0 CG2 A:THR508 4.8 45.4 1.0 O A:HOH854 4.9 54.0 1.0

Chlorine binding site 2 out of 3 in the Aged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1


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 Analogue TA1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl604 b:71.7 occ:1.00 O A:ASP378 3.0 75.1 1.0 CB A:GLN380 3.0 71.1 1.0 N A:ASP378 3.1 73.2 1.0 CG A:GLN380 3.4 72.4 1.0 C A:ASP378 3.4 74.5 1.0 CA A:ASP378 3.4 74.3 1.0 CG A:ARG381 3.6 67.3 1.0 N A:GLN380 3.7 71.6 1.0 CB A:ASP378 3.8 74.7 1.0 N A:ARG381 3.8 66.6 1.0 CA A:GLN380 3.9 70.4 1.0 C A:VAL377 4.3 71.8 1.0 N A:ASP379 4.4 74.3 1.0 C A:GLN380 4.4 69.0 1.0 CB A:ARG381 4.5 64.4 1.0 O A:VAL377 4.6 73.4 1.0 CD A:GLN380 4.7 76.2 1.0 CD A:ARG381 4.7 71.7 1.0 CA A:ARG381 4.8 64.1 1.0 C A:ASP379 4.9 72.8 1.0

Chlorine binding site 3 out of 3 in the Aged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Aged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl606 b:63.0 occ:1.00 O A:HOH1039 2.9 62.1 1.0 N A:ARG515 3.1 21.4 1.0 O A:HOH708 3.2 44.4 1.0 CA A:ARG515 3.6 24.4 1.0 O4 A:SO4605 3.8 52.0 0.8 NH2 A:ARG515 3.8 37.0 1.0 CD A:ARG515 4.0 34.1 1.0 CG A:ARG515 4.2 27.4 1.0 CD1 A:LEU514 4.2 18.7 1.0 C A:LEU514 4.2 19.7 1.0 O A:HOH821 4.4 22.5 1.0 CA A:LEU514 4.5 19.8 1.0 CB A:ARG515 4.5 26.1 1.0 O A:HOH865 4.5 34.4 1.0 O A:HOH933 4.6 64.5 1.0 C A:ARG515 4.8 24.9 1.0 NE2 A:GLN518 4.9 32.6 1.0 CZ A:ARG515 4.9 39.4 1.0 OE1 A:GLN518 4.9 32.4 1.0 NE A:ARG515 4.9 30.0 1.0 CG A:LEU514 4.9 20.9 1.0 N A:ALA516 5.0 26.7 1.0

E.Carletti, N.Aurbek, E.Gillon, M.Loiodice, Y.Nicolet, J.C.Fontecilla-Camps, P.Masson, H.Thiermann, F.Nachon, F.Worek. Structure-Activity Analysis of Aging and Reactivation of Human Butyrylcholinesterase Inhibited By Analogues of Tabun. Biochem. J. V. 421 97 2009.
ISSN: ESSN 1470-8728
PubMed: 19368529
DOI: 10.1042/BJ20090091