Chlorine in PDB 6g4m: Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 1

All present enzymatic activity of Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 1:
3.1.1.7;

The structure of Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 1, PDB code: 6g4m 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)	45.91 / 2.63
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	91.276, 106.240, 150.456, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 26.5

The binding sites of Chlorine atom in the Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 1 (pdb code 6g4m). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Torpedo Californica Acetylcholinesterase Bound to Uncharged Hybrid Reactivator 1, PDB code: 6g4m:

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


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 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl605 b:54.2 occ:1.00 O A:HOH831 2.3 58.1 1.0 O A:HOH909 2.8 37.4 1.0 O A:LEU256 3.6 38.4 1.0 CG2 A:VAL246 3.6 27.9 1.0 OD1 A:ASP259 3.7 52.5 1.0 C A:SER258 4.7 44.1 1.0 C A:LEU256 4.7 38.5 1.0 N A:ASP259 4.8 37.8 1.0 CD2 A:LEU262 4.8 35.5 1.0 CB A:VAL246 4.9 29.4 1.0 CG1 A:VAL246 4.9 33.5 1.0 N A:SER258 4.9 41.8 1.0 CD2 A:LEU158 4.9 36.3 1.0 CG A:ASP259 4.9 43.7 1.0 O A:SER258 4.9 42.7 1.0 CA A:SER258 4.9 46.8 1.0 O A:HOH889 5.0 43.9 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