Zinc in PDB 6eqp: Human Butyrylcholinesterase in Complex with Ethopropazine

All present enzymatic activity of Human Butyrylcholinesterase in Complex with Ethopropazine:
3.1.1.8;

The structure of Human Butyrylcholinesterase in Complex with Ethopropazine, PDB code: 6eqp was solved by F.Nachon, X.Brazzolotto, M.Wandhammer, M.Trovaslet-Leroy, T.L.Rosenberry, I.R.Macdonald, S.Darvesh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.88 / 2.35
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	155.230, 155.230, 135.300, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 23.7

The structure of Human Butyrylcholinesterase in Complex with Ethopropazine also contains other interesting chemical elements:

Chlorine

(Cl)

7 atoms

The binding sites of Zinc atom in the Human Butyrylcholinesterase in Complex with Ethopropazine (pdb code 6eqp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Human Butyrylcholinesterase in Complex with Ethopropazine, PDB code: 6eqp:

Zinc binding site 1 out of 1 in the Human Butyrylcholinesterase in Complex with Ethopropazine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Butyrylcholinesterase in Complex with Ethopropazine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn620 b:95.7 occ:1.00 C22 A:BUW601 3.2 75.3 0.5 C17 A:BUW601 3.4 75.6 0.5 OE2 A:GLU197 4.0 34.8 1.0 N A:GLY116 4.2 35.1 1.0 O A:HOH891 4.3 64.6 1.0 O A:HOH712 4.3 39.1 1.0 C21 A:BUW601 4.3 73.8 0.5 CA A:GLY116 4.3 35.2 1.0 CE3 A:TRP82 4.4 35.6 1.0 C A:GLY115 4.5 36.6 1.0 CZ3 A:TRP82 4.5 35.7 1.0 O A:HOH784 4.5 52.1 1.0 O A:HOH782 4.6 35.9 1.0 C15 A:BUW601 4.7 76.2 0.5 CD2 A:TRP82 4.7 38.6 1.0 C16 A:BUW601 4.8 75.3 0.5 O A:GLY115 4.8 38.3 1.0 CB A:SER198 4.8 33.9 1.0 N18 A:BUW601 4.8 74.4 0.5 O A:HOH776 4.9 36.5 1.0 CD2 A:HIS438 4.9 35.7 1.0 CD A:GLU197 4.9 36.5 1.0 OE1 A:GLU197 4.9 35.9 1.0 OG A:SER198 4.9 34.2 1.0 CH2 A:TRP82 4.9 38.2 1.0 NE2 A:HIS438 5.0 36.2 1.0

T.L.Rosenberry, X.Brazzolotto, I.R.Macdonald, M.Wandhammer, M.Trovaslet-Leroy, S.Darvesh, F.Nachon. Comparison of the Binding of Reversible Inhibitors to Human Butyrylcholinesterase and Acetylcholinesterase: A Crystallographic, Kinetic and Calorimetric Study. Molecules V. 22 2017.
ISSN: ESSN 1420-3049
PubMed: 29186056
DOI: 10.3390/MOLECULES22122098