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Potassium in PDB 2xqf: X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx

Enzymatic activity of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx

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

Protein crystallography data

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx, PDB code: 2xqf 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) 48.00 / 2.10
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 155.110, 155.110, 128.100, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 18.9

Other elements in 2xqf:

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

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

Potassium Binding Sites:

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

Potassium binding site 1 out of 1 in 2xqf

Go back to Potassium Binding Sites List in 2xqf
Potassium binding site 1 out of 1 in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Racemic Vx


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 Racemic Vx within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1535

b:89.4
occ:0.50
CZ A:PHE525 3.5 55.2 1.0
CE1 A:PHE525 3.6 54.3 1.0
CE2 A:PHE525 3.6 51.1 1.0
CD1 A:PHE525 3.9 54.5 1.0
CD2 A:PHE525 4.0 49.3 1.0
CG A:PHE525 4.0 50.4 1.0
CE1 A:HIS372 4.2 30.7 0.5
CZ A:PHE364 4.7 34.0 1.0
NE2 A:HIS372 4.9 32.6 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: Sun Dec 13 23:13:48 2020

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