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Potassium in PDB 2xqk: X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S)

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

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

Protein crystallography data

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S), PDB code: 2xqk 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) 41.53 / 2.40
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 154.920, 154.920, 127.390, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 21.7

Other elements in 2xqk:

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

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

Potassium Binding Sites:

The binding sites of Potassium atom in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S) (pdb code 2xqk). 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-(S), PDB code: 2xqk:

Potassium binding site 1 out of 1 in 2xqk

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


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-(S) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1538

b:91.3
occ:0.50
CZ A:PHE525 3.7 66.9 1.0
CE1 A:PHE525 3.8 66.8 1.0
CE2 A:PHE525 3.8 65.8 1.0
CD1 A:PHE525 3.9 67.8 1.0
CG A:PHE525 3.9 59.1 1.0
CD2 A:PHE525 3.9 60.2 1.0
CE1 A:HIS372 4.0 28.5 0.5
NE2 A:HIS372 4.6 28.4 0.5
CZ A:PHE364 4.7 35.9 1.0
CB A:PHE525 4.8 55.4 1.0
CB A:SER368 4.9 33.0 1.0
O3 A:SO41533 5.0 68.3 0.8

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 07:41:50 2024

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