Atomistry » Potassium » PDB 2w0f-2xo0 » 2xmc
Atomistry »
  Potassium »
    PDB 2w0f-2xo0 »
      2xmc »

Potassium in PDB 2xmc: G117H Mutant of Human Butyrylcholinesterase in Complex with Fluoride Anion

Enzymatic activity of G117H Mutant of Human Butyrylcholinesterase in Complex with Fluoride Anion

All present enzymatic activity of G117H Mutant of Human Butyrylcholinesterase in Complex with Fluoride Anion:
3.1.1.8;

Protein crystallography data

The structure of G117H Mutant of Human Butyrylcholinesterase in Complex with Fluoride Anion, PDB code: 2xmc was solved by F.Nachon, E.Carletti, M.Wandhammer, Y.Nicolet, L.M.Schopfer, P.Masson, O.Lockridge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 109.76 / 2.40
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 155.590, 155.590, 127.990, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 25.3

Other elements in 2xmc:

The structure of G117H Mutant of Human Butyrylcholinesterase in Complex with Fluoride Anion also contains other interesting chemical elements:

Fluorine (F) 1 atom
Chlorine (Cl) 5 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the G117H Mutant of Human Butyrylcholinesterase in Complex with Fluoride Anion (pdb code 2xmc). 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 G117H Mutant of Human Butyrylcholinesterase in Complex with Fluoride Anion, PDB code: 2xmc:

Potassium binding site 1 out of 1 in 2xmc

Go back to Potassium Binding Sites List in 2xmc
Potassium binding site 1 out of 1 in the G117H Mutant of Human Butyrylcholinesterase in Complex with Fluoride Anion


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of G117H Mutant of Human Butyrylcholinesterase in Complex with Fluoride Anion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1553

b:79.7
occ:1.00
O A:HOH2212 2.9 24.3 1.0
N A:ARG515 3.5 33.4 1.0
CA A:ARG515 4.0 34.2 1.0
NH2 A:ARG515 4.2 44.7 1.0
O A:HOH2215 4.2 47.2 1.0
O A:HOH2205 4.5 16.1 1.0
CD A:ARG515 4.5 36.6 1.0
O A:HOH2213 4.5 21.5 1.0
C A:LEU514 4.6 32.7 1.0
CG A:ARG515 4.7 31.7 1.0
CD1 A:LEU514 4.7 31.5 1.0
O A:HOH2204 4.8 46.7 1.0
CA A:LEU514 4.9 32.6 1.0
CB A:ARG515 4.9 33.0 1.0
NE2 A:GLN518 4.9 43.5 1.0
OE1 A:GLN518 5.0 47.0 1.0

Reference:

F.Nachon, E.Carletti, M.Wandhammer, Y.Nicolet, L.M.Schopfer, P.Masson, O.Lockridge. X-Ray Crystallographic Snapshots of Reaction Intermediates in the G117H Mutant of Human Butyrylcholinesterase, A Nerve Agent Target Engineered Into A Catalytic Bioscavenge Biochem.J. V. 434 73 2011.
ISSN: ISSN 0264-6021
PubMed: 21091433
DOI: 10.1042/BJ20101648
Page generated: Mon Aug 12 07:39:59 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy