Magnesium in PDB 3upy: Crystal Structure of the Brucella Abortus Enzyme Catalyzing the First Committed Step of the Methylerythritol 4-Phosphate Pathway.

The structure of Crystal Structure of the Brucella Abortus Enzyme Catalyzing the First Committed Step of the Methylerythritol 4-Phosphate Pathway., PDB code: 3upy was solved by B.M.Calisto, J.Perez-Gil, I.Fita, M.Rodriguez-Concepcion, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.55 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	49.391, 63.379, 79.334, 68.79, 75.54, 72.07
R / Rfree (%)	16.3 / 20.4

The binding sites of Magnesium atom in the Crystal Structure of the Brucella Abortus Enzyme Catalyzing the First Committed Step of the Methylerythritol 4-Phosphate Pathway. (pdb code 3upy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Brucella Abortus Enzyme Catalyzing the First Committed Step of the Methylerythritol 4-Phosphate Pathway., PDB code: 3upy:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Brucella Abortus Enzyme Catalyzing the First Committed Step of the Methylerythritol 4-Phosphate Pathway.


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 Brucella Abortus Enzyme Catalyzing the First Committed Step of the Methylerythritol 4-Phosphate Pathway. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg446 b:2.4 occ:1.00 O1 A:FOM447 1.9 13.3 0.8 OE1 A:GLU168 2.0 10.4 1.0 O2 A:FOM447 2.0 14.5 0.8 OD1 A:ASP167 2.0 12.2 1.0 OE2 A:GLU232 2.1 11.9 1.0 O A:HOH467 2.1 10.0 1.0 N1 A:FOM447 2.5 25.8 0.8 C1 A:FOM447 2.5 23.1 0.8 CD A:GLU168 3.0 10.1 1.0 CD A:GLU232 3.0 9.9 1.0 CG A:ASP167 3.2 11.5 1.0 OE2 A:GLU168 3.4 12.9 1.0 OE1 A:GLU232 3.4 12.0 1.0 OD2 A:ASP167 3.7 14.5 1.0 O A:HOH655 3.8 31.0 1.0 C2 A:FOM447 3.9 26.7 0.8 O A:HOH457 3.9 32.1 1.0 N A:GLU168 4.1 10.7 1.0 CG A:GLU232 4.3 10.9 1.0 CG A:GLU168 4.3 10.9 1.0 NE2 A:HIS323 4.4 17.7 0.8 CB A:ASP167 4.4 10.3 1.0 C3 A:FOM447 4.5 26.1 0.8 CA A:ASP167 4.6 9.5 1.0 CB A:GLU168 4.6 9.1 1.0 CE1 A:HIS323 4.6 14.3 0.2 CG A:LYS228 4.7 15.9 1.0 CD2 A:HIS323 4.7 13.4 0.8 CD A:LYS228 4.8 18.8 1.0 C A:ASP167 4.9 8.3 1.0 NZ A:LYS191 4.9 15.3 1.0 ND1 A:HIS323 5.0 12.1 0.2

Magnesium binding site 2 out of 2 in the Crystal Structure of the Brucella Abortus Enzyme Catalyzing the First Committed Step of the Methylerythritol 4-Phosphate Pathway.


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 Brucella Abortus Enzyme Catalyzing the First Committed Step of the Methylerythritol 4-Phosphate Pathway. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg446 b:7.0 occ:1.00 O B:HOH666 2.0 11.8 1.0 OE2 B:GLU232 2.0 11.9 1.0 OE1 B:GLU168 2.0 11.2 1.0 O B:HOH664 2.1 7.9 1.0 OD1 B:ASP167 2.1 14.1 1.0 O B:HOH665 2.2 12.6 1.0 CD B:GLU168 3.1 12.6 1.0 CD B:GLU232 3.1 11.0 1.0 CG B:ASP167 3.2 14.7 1.0 OE2 B:GLU168 3.4 13.3 1.0 OE1 B:GLU232 3.5 12.3 1.0 O B:HOH525 3.7 30.3 1.0 OD2 B:ASP167 3.8 14.2 1.0 O B:HOH524 3.8 32.1 1.0 N B:GLU168 4.1 9.1 1.0 CG B:GLU168 4.3 12.8 1.0 CG B:GLU232 4.4 10.2 1.0 CB B:ASP167 4.5 11.2 1.0 CE1 B:HIS323 4.5 18.2 1.0 CA B:ASP167 4.6 10.4 1.0 CB B:GLU168 4.6 10.3 1.0 CG B:LYS228 4.7 16.3 1.0 CD B:LYS228 4.7 17.4 1.0 NZ B:LYS191 4.8 15.7 1.0 C B:ASP167 4.9 10.0 1.0 ND1 B:HIS323 5.0 16.4 1.0

J.Perez-Gil, B.M.Calisto, C.Behrendt, T.Kurz, I.Fita, M.Rodriguez-Concepcion. Crystal Structure of Brucella Abortus Deoxyxylulose-5-Phosphate Reductoisomerase-Like (Drl) Enzyme Involved in Isoprenoid Biosynthesis. J.Biol.Chem. V. 287 15803 2012.
ISSN: ISSN 0021-9258
PubMed: 22442144
DOI: 10.1074/JBC.M112.354811