Magnesium in PDB 1ovd: The K136E Mutant of Lactococcus Lactis Dihydroorotate Dehydrogenase A in Complex with Orotate

All present enzymatic activity of The K136E Mutant of Lactococcus Lactis Dihydroorotate Dehydrogenase A in Complex with Orotate:
1.3.3.1;

The structure of The K136E Mutant of Lactococcus Lactis Dihydroorotate Dehydrogenase A in Complex with Orotate, PDB code: 1ovd was solved by S.Norager, S.Arent, O.Bjornberg, M.Ottosen, L.Lo Leggio, K.F.Jensen, S.Larsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 2.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.870, 108.290, 65.940, 90.00, 103.85, 90.00
R / Rfree (%)	17.8 / 20.2

The binding sites of Magnesium atom in the The K136E Mutant of Lactococcus Lactis Dihydroorotate Dehydrogenase A in Complex with Orotate (pdb code 1ovd). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The K136E Mutant of Lactococcus Lactis Dihydroorotate Dehydrogenase A in Complex with Orotate, PDB code: 1ovd:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The K136E Mutant of Lactococcus Lactis Dihydroorotate Dehydrogenase A in Complex with Orotate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The K136E Mutant of Lactococcus Lactis Dihydroorotate Dehydrogenase A in Complex with Orotate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg850 b:24.9 occ:1.00 O A:LYS33 2.2 16.8 1.0 O A:HOH988 2.4 29.8 1.0 O A:SER35 2.5 16.7 1.0 O A:HOH1152 2.5 38.1 1.0 O A:HOH907 2.6 15.2 1.0 O A:HOH1074 2.9 32.2 1.0 C A:LYS33 3.3 17.2 1.0 C A:SER35 3.7 17.3 1.0 O A:HOH1133 3.8 34.5 1.0 C A:ALA34 4.0 17.4 1.0 O A:HOH954 4.0 19.0 1.0 N A:SER35 4.0 17.3 1.0 O A:ALA37 4.2 13.9 1.0 N A:ALA34 4.2 17.0 1.0 O A:LEU32 4.2 16.7 1.0 CA A:LYS33 4.2 17.7 1.0 O A:ALA34 4.3 17.8 1.0 CA A:ALA34 4.3 17.1 1.0 CA A:SER35 4.5 17.2 1.0 O A:HOH1039 4.5 22.6 1.0 N A:GLN36 4.6 17.3 1.0 O A:HOH1147 4.7 40.9 1.0 CA A:GLN36 4.7 17.4 1.0 C A:GLN36 4.9 16.6 1.0 N A:ALA37 4.9 15.7 1.0

Magnesium binding site 2 out of 2 in the The K136E Mutant of Lactococcus Lactis Dihydroorotate Dehydrogenase A in Complex with Orotate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The K136E Mutant of Lactococcus Lactis Dihydroorotate Dehydrogenase A in Complex with Orotate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg851 b:22.9 occ:1.00 O B:LYS33 2.2 17.6 1.0 O B:HOH1066 2.4 31.3 1.0 O B:SER35 2.5 17.7 1.0 O B:HOH1071 2.6 24.0 1.0 O B:HOH985 2.6 14.5 1.0 C B:LYS33 3.4 17.8 1.0 C B:SER35 3.7 17.6 1.0 C B:ALA34 3.9 17.6 1.0 O B:HOH1032 4.0 19.3 1.0 N B:SER35 4.0 17.4 1.0 O B:ALA37 4.1 14.3 1.0 O B:ALA34 4.2 18.0 1.0 O B:LEU32 4.2 16.8 1.0 N B:ALA34 4.2 17.2 1.0 CA B:ALA34 4.3 17.5 1.0 CA B:LYS33 4.3 18.1 1.0 CA B:SER35 4.5 17.3 1.0 O B:HOH948 4.6 21.9 1.0 N B:GLN36 4.6 17.8 1.0 CA B:GLN36 4.7 18.1 1.0 C B:GLN36 4.9 17.2 1.0 N B:ALA37 4.9 16.4 1.0 CG B:LYS33 5.0 22.1 1.0

S.Norager, S.Arent, O.Bjornberg, M.Ottesen, L.Lo Leggio, K.F.Jensen, S.Larsen. Lactococcus Lactis Dihydroorotate Dehydrogenase A Mutants Reveal Important Facets of the Enzymatic Function. J.Biol.Chem. V. 278 28812 2003.
ISSN: ISSN 0021-9258
PubMed: 12732650
DOI: 10.1074/JBC.M303767200