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Atomistry » Chlorine » PDB 4ms0-4mye » 4mus » |
Chlorine in PDB 4mus: Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate AnalogProtein crystallography data
The structure of Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog, PDB code: 4mus
was solved by
P.J.Stogios,
E.Evdokimova,
D.Meziane-Cherif,
R.Di Leo,
V.Yim,
P.Courvalin,
A.Savchenko,
W.F.Anderson,
Center For Structural Genomics Ofinfectious Diseases (Csgid),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4mus:
The structure of Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog
(pdb code 4mus). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog, PDB code: 4mus: Chlorine binding site 1 out of 1 in 4musGo back to Chlorine Binding Sites List in 4mus
Chlorine binding site 1 out
of 1 in the Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Ala-D-Ala Phosphinate Analog
Mono view Stereo pair view
Reference:
D.Meziane-Cherif,
P.J.Stogios,
E.Evdokimova,
A.Savchenko,
P.Courvalin.
Structural Basis For the Evolution of Vancomycin Resistance D,D-Peptidases. Proc.Natl.Acad.Sci.Usa V. 111 5872 2014.
Page generated: Sat Dec 12 10:56:49 2020
ISSN: ISSN 0027-8424 PubMed: 24711382 DOI: 10.1073/PNAS.1402259111 |
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