Atomistry » Magnesium » PDB 2xni-2xzs » 2xqj
Atomistry »
  Magnesium »
    PDB 2xni-2xzs »
      2xqj »

Magnesium in PDB 2xqj: X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R)

Enzymatic activity of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R)

All present enzymatic activity of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R):
3.1.1.8;

Protein crystallography data

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R), PDB code: 2xqj 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) 49.27 / 2.40
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 155.820, 155.820, 128.280, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 22.3

Other elements in 2xqj:

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R) also contains other interesting chemical elements:

Sodium (Na) 2 atoms
Chlorine (Cl) 2 atoms
Calcium (Ca) 2 atoms
Potassium (K) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R) (pdb code 2xqj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R), PDB code: 2xqj:

Magnesium binding site 1 out of 1 in 2xqj

Go back to Magnesium Binding Sites List in 2xqj
Magnesium binding site 1 out of 1 in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1550

b:66.8
occ:1.00
O A:HOH2091 1.8 47.3 1.0
O A:HOH2004 2.4 32.6 1.0
O A:HOH2015 3.4 27.1 1.0
C1 A:VX1530 3.8 25.8 0.9
CE3 A:TRP82 4.1 23.3 1.0
CD2 A:TRP82 4.1 25.4 1.0
CG A:TRP82 4.4 30.7 1.0
CZ3 A:TRP82 4.6 25.6 1.0
CE2 A:TRP82 4.6 26.7 1.0
CD2 A:HIS438 4.7 26.5 1.0
CB A:TRP82 4.8 31.2 1.0
NE2 A:HIS438 4.9 27.4 1.0
CD1 A:TRP82 5.0 30.5 1.0

Reference:

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
Page generated: Sun Aug 10 16:31:02 2025

Last articles

Mn in 9FZ6
Mn in 9G1C
Mn in 9G1A
Mn in 9ERF
Mn in 9F6P
Mn in 9F6N
Mn in 9EVJ
Mn in 9ETK
Mn in 9ERE
Mn in 9EJ5
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy