Magnesium in PDB 3upl: 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: 3upl 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)	25.00 / 1.50
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	49.365, 63.380, 79.123, 68.63, 75.80, 72.70
R / Rfree (%)	15 / 17.6

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 3upl). 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: 3upl:
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:Mg447 b:6.6 occ:1.00 OE2 A:GLU232 2.0 7.7 1.0 OD1 A:ASP167 2.0 8.4 1.0 OE1 A:GLU168 2.0 8.5 1.0 O A:HOH452 2.1 8.1 1.0 O A:HOH539 2.1 10.6 1.0 O A:HOH588 2.1 7.8 1.0 CD A:GLU168 3.1 8.4 1.0 CD A:GLU232 3.1 8.2 1.0 CG A:ASP167 3.2 9.0 1.0 OE2 A:GLU168 3.5 10.2 1.0 OE1 A:GLU232 3.5 7.6 1.0 OD2 A:ASP167 3.8 11.7 1.0 O A:HOH636 3.8 28.1 1.0 O A:HOH755 3.9 19.4 1.0 N A:GLU168 4.1 6.1 1.0 O A:HOH884 4.2 32.1 1.0 CG A:GLU232 4.3 5.0 1.0 CG A:GLU168 4.4 7.8 1.0 CB A:ASP167 4.4 7.3 1.0 NE2 A:HIS323 4.5 9.0 0.5 CE1 A:HIS323 4.5 13.5 0.5 CA A:ASP167 4.6 5.6 1.0 CB A:GLU168 4.6 7.7 1.0 CD A:LYS228 4.7 13.0 1.0 CG A:LYS228 4.7 10.3 1.0 C A:ASP167 4.8 6.6 1.0 CD2 A:HIS323 4.9 8.3 0.5 NZ A:LYS191 4.9 11.2 1.0 CA A:GLU168 5.0 7.9 1.0

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:Mg447 b:6.4 occ:1.00 OD1 B:ASP167 2.0 6.8 1.0 OE2 B:GLU232 2.0 7.7 1.0 OE1 B:GLU168 2.1 7.3 1.0 O B:HOH561 2.1 2.0 1.0 O B:HOH574 2.1 2.4 1.0 O B:HOH562 2.1 4.8 1.0 CD B:GLU232 3.1 7.1 1.0 CD B:GLU168 3.1 8.5 1.0 CG B:ASP167 3.2 7.9 1.0 OE2 B:GLU168 3.5 9.8 1.0 OE1 B:GLU232 3.6 8.2 1.0 OD2 B:ASP167 3.8 10.6 1.0 O B:HOH660 3.8 10.8 1.0 O B:HOH829 3.8 17.0 1.0 N B:GLU168 4.1 5.0 1.0 O B:HOH855 4.3 21.5 1.0 CG B:GLU232 4.3 4.5 1.0 CG B:GLU168 4.4 7.0 1.0 CB B:ASP167 4.4 5.7 1.0 NE2 B:HIS323 4.4 13.3 0.5 CA B:ASP167 4.6 5.7 1.0 CE1 B:HIS323 4.6 11.4 0.5 CD B:LYS228 4.7 12.4 1.0 CB B:GLU168 4.7 7.4 1.0 CG B:LYS228 4.7 11.5 1.0 NZ B:LYS191 4.8 10.7 1.0 C B:ASP167 4.8 6.8 1.0 CD2 B:HIS323 4.9 11.2 0.5 CA B:GLU168 5.0 5.4 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