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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: Mon Dec 14 07:47:10 2020

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