Calcium in PDB 2xqg: X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr

All present enzymatic activity of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr:
3.1.1.8;

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr, PDB code: 2xqg was solved by M.Wandhammer, E.Carletti, E.Gillon, P.Masson, M.Goeldner, D.Noort, F.Nachon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.51 / 2.30
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	154.600, 154.600, 127.610, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 21.5

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr also contains other interesting chemical elements:

Bromine	(Br)	1 atom
Sodium	(Na)	2 atoms
Chlorine	(Cl)	1 atom

The binding sites of Calcium atom in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr (pdb code 2xqg). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr, PDB code: 2xqg:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1551 b:73.4 occ:1.00 O A:HOH2040 2.2 31.8 1.0 O A:HOH2179 2.8 31.2 1.0 O A:HOH2335 3.3 26.5 1.0 O A:HOH2016 3.8 38.8 1.0 CD2 A:TRP82 3.8 24.2 1.0 CE3 A:TRP82 4.0 20.4 1.0 CE2 A:TRP82 4.0 25.8 1.0 C1 A:VR1530 4.1 16.4 1.0 CD2 A:HIS438 4.1 31.8 1.0 O A:HOH2041 4.2 48.0 1.0 CZ3 A:TRP82 4.2 21.1 1.0 CZ2 A:TRP82 4.2 29.6 1.0 CG A:TRP82 4.3 26.6 1.0 CH2 A:TRP82 4.3 27.7 1.0 NE2 A:HIS438 4.4 31.2 1.0 NE1 A:TRP82 4.4 23.8 1.0 CD1 A:TRP82 4.6 28.2 1.0 OE1 A:GLU197 4.9 21.5 1.0 CA A:GLY439 4.9 23.4 1.0 OE2 A:GLU197 5.0 23.4 1.0 CB A:TRP82 5.0 26.4 1.0

Calcium binding site 2 out of 3 in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1552 b:61.3 occ:1.00 O A:HOH2355 2.9 33.2 1.0 OG1 A:THR508 3.4 53.4 1.0 CB A:THR508 3.7 46.6 1.0 N A:THR488 3.7 46.4 1.0 OG1 A:THR488 3.8 45.6 1.0 CA A:SER487 3.9 52.1 1.0 CB A:SER487 4.0 50.2 1.0 O A:HOH2369 4.3 19.9 1.0 OG A:SER487 4.3 55.4 1.0 C A:SER487 4.4 49.7 1.0 CG2 A:THR508 4.4 45.5 1.0 CB A:THR488 4.5 41.9 1.0 N A:THR508 4.7 47.5 1.0 CA A:THR488 4.7 43.1 1.0 O A:GLN486 4.8 60.7 1.0 CA A:THR508 4.9 45.7 1.0 NH1 A:ARG470 4.9 24.3 1.0

Calcium binding site 3 out of 3 in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vr within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1553 b:66.2 occ:1.00 OH A:TYR420 3.2 29.6 1.0 O A:HOH2322 3.3 33.1 1.0 CE A:LYS323 3.9 41.7 1.0 NH2 A:ARG515 4.0 36.3 1.0 CZ A:TYR420 4.2 31.4 1.0 CG A:LYS323 4.2 28.6 1.0 CE2 A:TYR420 4.4 24.5 1.0 O A:HOH2304 4.4 32.5 1.0 CD A:LYS323 4.4 34.1 1.0 O A:HOH2402 4.5 20.4 1.0 NZ A:LYS323 4.5 51.3 1.0 NH1 A:ARG515 4.6 25.9 1.0 CZ A:ARG515 4.7 36.5 1.0 O A:HOH2387 4.9 32.2 1.0 O A:HOH2256 4.9 46.5 1.0

M.Wandhammer, E.Carletti, M.Van Der Schans, E.Gillon, Y.Nicolet, P.Masson, M.Goeldner, D.Noort, F.Nachon. Structural Study of the Complex Stereoselectivity of Human Butyrylcholinesterase For the Neurotoxic V-Agents. J.Biol.Chem. V. 286 16783 2011.
ISSN: ISSN 0021-9258
PubMed: 21454498
DOI: 10.1074/JBC.M110.209569