Chlorine in PDB 6g4n: Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2

All present enzymatic activity of Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2:
3.1.1.7;

The structure of Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2, PDB code: 6g4n was solved by G.Santoni, E.De La Mora, J.De Souza, I.Silman, J.Sussman, R.Baati, M.Weik, F.Nachon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.29 / 2.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	91.807, 107.208, 150.450, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 27.1

The binding sites of Chlorine atom in the Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2 (pdb code 6g4n). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2, PDB code: 6g4n:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl603 b:87.2 occ:0.99 CL2 A:E2W603 0.0 87.2 1.0 C2 A:E2W603 1.7 71.4 1.0 C3 A:E2W603 2.7 59.6 1.0 C1 A:E2W603 2.7 60.7 1.0 OH A:TYR70 3.6 49.0 1.0 CE2 A:TYR70 3.6 45.0 1.0 CZ A:TYR70 3.8 43.1 1.0 C6 A:E2W603 4.0 55.6 1.0 C4 A:E2W603 4.0 56.2 1.0 O A:HOH815 4.0 47.9 1.0 C21 A:E2W603 4.2 55.5 1.0 OH A:TYR121 4.2 42.1 1.0 CZ2 A:TRP279 4.3 45.4 1.0 O A:HOH837 4.3 16.7 1.0 CD2 A:TYR70 4.5 40.6 1.0 C5 A:E2W603 4.5 53.1 1.0 CD2 A:TYR334 4.6 43.4 1.0 C20 A:E2W603 4.7 51.4 1.0 CH2 A:TRP279 4.8 46.1 1.0 CE1 A:TYR70 4.8 34.5 1.0 C22 A:E2W603 4.8 57.0 1.0 CE2 A:TRP279 4.8 38.7 1.0 CZ A:TYR121 4.9 36.6 1.0 O26 A:E2W603 5.0 59.3 1.0

Chlorine binding site 2 out of 3 in the Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl603 b:79.1 occ:1.00 CL2 B:E2W603 0.0 79.1 1.0 C2 B:E2W603 1.7 59.6 1.0 C3 B:E2W603 2.6 46.3 1.0 C1 B:E2W603 2.7 44.6 1.0 CZ2 B:TRP279 3.6 35.7 1.0 O B:HOH845 3.9 15.2 1.0 CH2 B:TRP279 3.9 42.8 1.0 C6 B:E2W603 3.9 40.9 1.0 C4 B:E2W603 3.9 38.6 1.0 O B:HOH734 4.0 61.6 1.0 OH B:TYR121 4.1 33.5 1.0 CE2 B:TYR70 4.1 40.2 1.0 OH B:TYR70 4.2 40.1 1.0 CE2 B:TRP279 4.3 32.9 1.0 CZ B:TYR70 4.3 43.5 1.0 C5 B:E2W603 4.5 39.7 1.0 C10 B:E2W603 4.5 85.7 1.0 N25 B:E2W603 4.5 88.8 1.0 CZ B:TYR121 4.6 41.9 1.0 CZ3 B:TRP279 4.7 41.9 1.0 NE1 B:TRP279 4.8 34.8 1.0 CD2 B:TYR70 4.8 37.6 1.0 CD2 B:TYR334 4.9 34.7 1.0

Chlorine binding site 3 out of 3 in the Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl604 b:63.2 occ:1.00 OD1 B:ASP389 4.0 52.6 1.0 OD2 B:ASP326 4.1 44.8 1.0 NZ B:LYS325 4.1 52.4 1.0 O B:TRP435 4.2 41.3 1.0 O B:HOH834 4.6 54.2 1.0 O B:GLU434 4.7 24.3 1.0 CG B:ASP389 4.8 45.0 1.0 C B:TRP435 4.8 28.8 1.0 NH1 B:ARG388 4.9 40.2 1.0 CE B:LYS325 4.9 54.6 1.0 CA B:GLY437 4.9 37.5 1.0

G.Santoni, J.De Sousa, E.De La Mora, J.Dias, L.Jean, J.L.Sussman, I.Silman, P.Y.Renard, R.C.D.Brown, M.Weik, R.Baati, F.Nachon. Structure-Based Optimization of Nonquaternary Reactivators of Acetylcholinesterase Inhibited By Organophosphorus Nerve Agents. J. Med. Chem. V. 61 7630 2018.
ISSN: ISSN 1520-4804
PubMed: 30125110
DOI: 10.1021/ACS.JMEDCHEM.8B00592