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Potassium 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
Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium 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 Potassium atom.
In total only one binding site of Potassium was determined in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(R), PDB code: 2xqj:

Potassium binding site 1 out of 1 in 2xqj

Go back to Potassium Binding Sites List in 2xqj
Potassium 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 Potassium with other atoms in the K 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:K1534

b:87.5
occ:0.50
CZ A:PHE525 3.6 62.3 1.0
CE2 A:PHE525 3.7 60.3 1.0
CE1 A:PHE525 3.8 62.9 1.0
CD1 A:PHE525 4.0 62.6 1.0
CD2 A:PHE525 4.0 56.1 1.0
CG A:PHE525 4.1 55.9 1.0
CE1 A:HIS372 4.2 29.7 0.5
CZ A:PHE364 4.5 36.2 1.0
CB A:SER368 4.7 33.7 1.0
NE2 A:HIS372 4.8 28.6 0.5

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 Aug 12 07:41:49 2024

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