Chlorine in PDB 6f7q: Human Butyrylcholinesterase Complexed with N-Propargyliperidines

All present enzymatic activity of Human Butyrylcholinesterase Complexed with N-Propargyliperidines:
3.1.1.8;

The structure of Human Butyrylcholinesterase Complexed with N-Propargyliperidines, PDB code: 6f7q was solved by N.Coquelle, D.Knez, J.P.Colletier, S.Gobec, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.11 / 2.60
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	152.140, 152.140, 141.910, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 24.8

The binding sites of Chlorine atom in the Human Butyrylcholinesterase Complexed with N-Propargyliperidines (pdb code 6f7q). 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 Human Butyrylcholinesterase Complexed with N-Propargyliperidines, PDB code: 6f7q:

Chlorine binding site 1 out of 1 in the Human Butyrylcholinesterase Complexed with N-Propargyliperidines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Butyrylcholinesterase Complexed with N-Propargyliperidines within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl603 b:78.6 occ:1.00 N B:ARG515 3.2 61.4 1.0 CA B:ARG515 3.7 57.7 1.0 O B:HOH724 3.7 43.4 1.0 C B:LEU514 4.3 58.4 1.0 O B:LYS513 4.3 56.2 1.0 CG B:ARG515 4.4 63.8 1.0 NH2 B:ARG515 4.5 86.3 1.0 CA B:LEU514 4.5 50.1 1.0 O B:HOH736 4.5 53.0 1.0 N B:ALA516 4.5 55.2 1.0 C B:ARG515 4.7 57.3 1.0 CB B:ARG515 4.7 62.0 1.0 CD1 B:LEU514 4.8 54.2 1.0 OE1 B:GLN518 4.9 66.4 1.0

D.Knez, N.Coquelle, A.Pislar, S.Zakelj, M.Jukic, M.Sova, J.Mravljak, F.Nachon, X.Brazzolotto, J.Kos, J.P.Colletier, S.Gobec. Multi-Target-Directed Ligands For Treating Alzheimer'S Disease: Butyrylcholinesterase Inhibitors Displaying Antioxidant and Neuroprotective Activities. Eur.J.Med.Chem. V. 156 598 2018.
ISSN: ISSN 0223-5234
PubMed: 30031971
DOI: 10.1016/J.EJMECH.2018.07.033