Bromine in PDB 6eqq: Human Butyrylcholinesterase in Complex with Huprine 19

All present enzymatic activity of Human Butyrylcholinesterase in Complex with Huprine 19:
3.1.1.8;

The structure of Human Butyrylcholinesterase in Complex with Huprine 19, PDB code: 6eqq 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)	57.13 / 2.40
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	154.297, 154.297, 134.110, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 19.6

The structure of Human Butyrylcholinesterase in Complex with Huprine 19 also contains other interesting chemical elements:

Chlorine

(Cl)

5 atoms

The binding sites of Bromine atom in the Human Butyrylcholinesterase in Complex with Huprine 19 (pdb code 6eqq). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Human Butyrylcholinesterase in Complex with Huprine 19, PDB code: 6eqq:

Bromine binding site 1 out of 1 in the Human Butyrylcholinesterase in Complex with Huprine 19


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Human Butyrylcholinesterase in Complex with Huprine 19 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br611 b:84.1 occ:1.00 O A:HOH774 3.0 64.3 1.0 OG A:SER198 3.1 47.0 1.0 N A:GLY116 3.4 44.7 1.0 CB A:SER198 3.5 32.8 1.0 C08 A:H19601 3.5 59.2 1.0 N A:GLY117 3.7 46.1 1.0 NE2 A:HIS438 3.7 49.1 1.0 N10 A:H19601 3.7 61.9 1.0 CA A:GLY116 3.7 42.1 1.0 O A:HOH859 3.8 67.4 1.0 C A:GLY116 4.1 44.9 1.0 C09 A:H19601 4.1 58.3 1.0 O5 A:UNL623 4.3 69.6 1.0 C A:GLY115 4.4 39.3 1.0 CD2 A:HIS438 4.5 40.7 1.0 C06 A:H19601 4.6 61.1 1.0 N A:ALA199 4.6 36.0 1.0 O A:HOH905 4.6 59.0 1.0 CA A:GLY117 4.6 38.5 1.0 CE1 A:HIS438 4.7 40.8 1.0 OE1 A:GLU197 4.7 45.5 1.0 CA A:GLY115 4.7 37.3 1.0 C11 A:H19601 4.8 54.4 1.0 CL A:H19601 4.9 58.4 1.0 CA A:SER198 4.9 41.9 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