Magnesium in PDB 4ee6: Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated)

The structure of Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated), PDB code: 4ee6 was solved by G.Zocher, T.Stehle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.93 / 1.33
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.140, 135.600, 48.530, 90.00, 95.73, 90.00
R / Rfree (%)	19 / 21.3

The structure of Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated) also contains other interesting chemical elements:

Chlorine

(Cl)

12 atoms

The binding sites of Magnesium atom in the Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated) (pdb code 4ee6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated), PDB code: 4ee6:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated)


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 the Novel Phenazine Prenyltransferase Epzp (Methylated) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:13.9 occ:1.00 O A:HOH885 1.8 15.7 1.0 O A:HOH886 2.0 15.5 1.0 O B:HOH729 2.1 15.0 1.0 O A:HOH638 2.1 13.9 1.0 O A:HOH644 2.2 14.6 1.0 O B:HOH778 3.9 18.2 1.0 O A:GLU125 4.0 14.7 1.0 OD1 A:ASP181 4.2 16.6 1.0 OE2 B:GLU214 4.2 12.3 1.0 O B:HOH716 4.2 14.8 1.0 CA A:GLU125 4.2 12.3 1.0 O A:VAL179 4.3 12.8 1.0 O A:ALA124 4.4 11.6 1.0 C A:GLU125 4.4 13.2 1.0 O B:HOH818 4.4 15.0 1.0 O B:HOH711 4.4 15.9 1.0 CA A:GLY180 4.6 11.2 1.0 N A:ASP181 4.7 10.6 1.0 O A:HOH576 4.8 14.2 1.0 CD B:GLU214 4.9 10.6 1.0 C A:GLY180 4.9 10.7 1.0 O B:HOH572 5.0 13.2 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:15.8 occ:1.00 O B:HOH839 2.0 19.3 1.0 O B:HOH801 2.2 17.2 1.0 O B:HOH618 2.3 14.7 1.0 O B:HOH627 3.1 15.7 1.0 O B:GLU125 3.9 15.5 1.0 O A:HOH660 4.0 15.1 1.0 OD1 B:ASP181 4.0 20.2 1.0 CA B:GLU125 4.2 15.1 1.0 OE2 A:GLU214 4.2 13.6 1.0 O B:ALA124 4.3 13.0 1.0 O B:HOH820 4.4 15.8 1.0 C B:GLU125 4.4 14.6 1.0 O B:VAL179 4.4 14.2 1.0 O A:HOH824 4.6 17.6 1.0 CA B:GLY180 4.6 12.2 1.0 N B:ASP181 4.7 13.4 1.0 O B:HOH615 4.8 13.8 1.0 O A:HOH613 4.8 14.1 1.0 C B:GLY180 4.9 11.1 1.0 CD A:GLU214 4.9 10.1 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:15.8 occ:1.00 O B:HOH897 2.0 17.3 1.0 O B:HOH894 2.0 17.2 1.0 O B:HOH893 2.0 13.0 1.0 O B:HOH850 2.1 17.4 1.0 O B:HOH843 2.2 17.8 1.0 O B:HOH539 4.0 12.7 1.0 N B:GLY266 4.0 18.1 1.0 O B:HOH577 4.1 11.8 1.0 OG1 B:THR264 4.2 13.4 1.0 O B:HOH846 4.3 17.2 1.0 O B:HOH733 4.3 14.9 1.0 OD1 B:ASP263 4.5 19.5 1.0 CA B:GLY266 4.5 16.3 1.0 N B:GLU265 4.6 17.3 1.0 C B:GLU265 5.0 16.8 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Novel Phenazine Prenyltransferase Epzp (Methylated) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:15.0 occ:1.00 O B:HOH898 2.0 15.7 1.0 O B:HOH899 2.1 17.8 1.0 O B:HOH687 2.1 13.2 1.0 OE2 B:GLU9 4.1 14.1 1.0 OE1 B:GLU9 4.1 14.1 1.0 OE1 B:GLN289 4.2 13.6 1.0 O B:HOH775 4.4 17.9 1.0 CD B:GLU9 4.5 12.8 1.0 O B:HOH785 4.6 17.1 1.0 OH B:TYR288 4.7 13.5 1.0 CD B:GLN289 4.9 11.9 1.0 O B:HOH669 5.0 15.8 1.0

G.Zocher, O.Saleh, J.B.Heim, D.A.Herbst, L.Heide, T.Stehle. Structure-Based Engineering Increased the Catalytic Turnover Rate of A Novel Phenazine Prenyltransferase. Plos One V. 7 48427 2012.
ISSN: ESSN 1932-6203
PubMed: 23119011
DOI: 10.1371/JOURNAL.PONE.0048427