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Atomistry » Chlorine » PDB 3ilj-3isv » 3iog | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 3ilj-3isv » 3iog » |
Chlorine in PDB 3iog: Crystal Structure of Cpha N220G Mutant with Inhibitor 18Enzymatic activity of Crystal Structure of Cpha N220G Mutant with Inhibitor 18
All present enzymatic activity of Crystal Structure of Cpha N220G Mutant with Inhibitor 18:
3.5.2.6; Protein crystallography data
The structure of Crystal Structure of Cpha N220G Mutant with Inhibitor 18, PDB code: 3iog
was solved by
H.Delbruck,
C.Bebrone,
K.M.V.Hoffmann,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3iog:
The structure of Crystal Structure of Cpha N220G Mutant with Inhibitor 18 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Cpha N220G Mutant with Inhibitor 18
(pdb code 3iog). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Cpha N220G Mutant with Inhibitor 18, PDB code: 3iog: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3iogGo back to![]() ![]()
Chlorine binding site 1 out
of 2 in the Crystal Structure of Cpha N220G Mutant with Inhibitor 18
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 2 in 3iogGo back to![]() ![]()
Chlorine binding site 2 out
of 2 in the Crystal Structure of Cpha N220G Mutant with Inhibitor 18
![]() Mono view ![]() Stereo pair view
Reference:
P.Lassaux,
M.Hamel,
M.Gulea,
H.Delbruck,
P.S.Mercuri,
L.Horsfall,
D.Dehareng,
M.Kupper,
J.-M.Frere,
K.Hoffmann,
M.Galleni,
C.Bebrone.
Mercaptophosphonate Compounds As Broad-Spectrum Inhibitors of the Metallo-Beta-Lactamases J.Med.Chem. V. 53 4862 2010.
Page generated: Fri Jul 11 06:29:05 2025
ISSN: ISSN 0022-2623 PubMed: 20527888 DOI: 10.1021/JM100213C |
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