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)

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:

Resolution Low / High (Å)	19.33 / 2.00
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	41.939, 43.083, 66.316, 80.53, 74.52, 64.01
R / Rfree (%)	18.9 / 23.5

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:

Copper	(Cu)	2 atoms
Chlorine	(Cl)	6 atoms

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 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

A full contact list of Magnesium with other atoms in the Mg binding site number 1 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) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg205 b:33.2 occ:1.00 OE2 B:GLU66 2.1 24.7 1.0 OE2 A:GLU66 2.1 27.9 1.0 O B:HOH420 2.2 53.7 1.0 O A:HOH352 2.2 28.6 1.0 O A:HOH326 2.3 28.2 1.0 O A:HOH415 2.4 48.1 1.0 CD A:GLU66 3.0 24.4 1.0 CD B:GLU66 3.0 23.5 1.0 OE1 A:GLU66 3.3 23.4 1.0 OE1 B:GLU66 3.3 25.5 1.0 O A:HOH342 3.8 35.9 1.0 O B:HOH434 3.9 36.9 1.0 O B:HOH326 3.9 25.1 1.0 CG A:GLU66 4.4 21.3 1.0 CG B:GLU66 4.4 21.7 1.0 O2 B:SO4205 4.7 63.1 1.0

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.
ISSN: ISSN 0027-8424
PubMed: 24711382
DOI: 10.1073/PNAS.1402259111