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Atomistry » Magnesium » PDB 4o5k-4ogq » 4oak » |
Magnesium in PDB 4oak: Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Alanine-D-Alanine and Copper (II)Protein crystallography data
The structure of Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Alanine-D-Alanine and Copper (II), PDB code: 4oak
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 4oak:
The structure of Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Alanine-D-Alanine and Copper (II) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Alanine-D-Alanine and Copper (II)
(pdb code 4oak). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Vancomycin Resistance D,D-Dipeptidase/D,D- Pentapeptidase Vanxyc D59S Mutant in Complex with D-Alanine-D-Alanine and Copper (II), PDB code: 4oak: Magnesium binding site 1 out of 1 in 4oakGo back to Magnesium Binding Sites List in 4oak
Magnesium 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-Alanine-D-Alanine and Copper (II)
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: Mon Dec 14 19:17:10 2020
ISSN: ISSN 0027-8424 PubMed: 24711382 DOI: 10.1073/PNAS.1402259111 |
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