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Atomistry » Sodium » PDB 2xjr-2xzi » 2xmd » |
Sodium in PDB 2xmd: G117H Mutant of Human Butyrylcholinesterase in Complex with EchothiophateEnzymatic activity of G117H Mutant of Human Butyrylcholinesterase in Complex with Echothiophate
All present enzymatic activity of G117H Mutant of Human Butyrylcholinesterase in Complex with Echothiophate:
3.1.1.8; Protein crystallography data
The structure of G117H Mutant of Human Butyrylcholinesterase in Complex with Echothiophate, PDB code: 2xmd
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:
Other elements in 2xmd:
The structure of G117H Mutant of Human Butyrylcholinesterase in Complex with Echothiophate also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the G117H Mutant of Human Butyrylcholinesterase in Complex with Echothiophate
(pdb code 2xmd). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the G117H Mutant of Human Butyrylcholinesterase in Complex with Echothiophate, PDB code: 2xmd: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 2xmdGo back to![]() ![]()
Sodium binding site 1 out
of 2 in the G117H Mutant of Human Butyrylcholinesterase in Complex with Echothiophate
![]() Mono view ![]() Stereo pair view
Sodium binding site 2 out of 2 in 2xmdGo back to![]() ![]()
Sodium binding site 2 out
of 2 in the G117H Mutant of Human Butyrylcholinesterase in Complex with Echothiophate
![]() Mono view ![]() Stereo pair view
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.
Page generated: Mon Oct 7 05:14:07 2024
ISSN: ISSN 0264-6021 PubMed: 21091433 DOI: 10.1042/BJ20101648 |
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