Magnesium in PDB 5grh: Crystal Structure of the Alpha Gamma Heterodimer of Human IDH3 in Complex with Mg(2+)

All present enzymatic activity of Crystal Structure of the Alpha Gamma Heterodimer of Human IDH3 in Complex with Mg(2+):
1.1.1.41;

The structure of Crystal Structure of the Alpha Gamma Heterodimer of Human IDH3 in Complex with Mg(2+), PDB code: 5grh was solved by T.Ma, Y.Peng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.71 / 2.80
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.397, 118.397, 143.163, 90.00, 90.00, 120.00
R / Rfree (%)	22.4 / 25.9

The binding sites of Magnesium atom in the Crystal Structure of the Alpha Gamma Heterodimer of Human IDH3 in Complex with Mg(2+) (pdb code 5grh). 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 the Alpha Gamma Heterodimer of Human IDH3 in Complex with Mg(2+), PDB code: 5grh:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Alpha Gamma Heterodimer of Human IDH3 in Complex with Mg(2+)


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 Alpha Gamma Heterodimer of Human IDH3 in Complex with Mg(2+) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:27.8 occ:1.00 OD1 A:ASP230 1.8 53.3 1.0 OD2 A:ASP234 2.5 43.7 1.0 CG A:ASP230 2.6 53.2 1.0 OD2 B:ASP215 2.6 52.2 1.0 OD2 A:ASP230 2.8 54.0 1.0 CG A:ASP234 3.6 43.5 1.0 CG B:ASP215 3.6 50.1 1.0 OD1 A:ASP234 3.9 45.4 1.0 CB A:ASP230 4.0 52.2 1.0 CB B:ASP215 4.0 48.2 1.0 NH2 A:ARG98 4.4 50.3 1.0 O A:ASP230 4.6 51.0 1.0 C A:ASP230 4.7 48.9 1.0 OD1 B:ASP215 4.7 51.6 1.0 CA A:ASP230 4.8 50.9 1.0 CB A:ASP234 4.9 42.7 1.0

T.Ma, Y.Peng, W.Huang, J.Ding. Molecular Mechanism of the Allosteric Regulation of the Alpha Gamma Heterodimer of Human Nad-Dependent Isocitrate Dehydrogenase. Sci Rep V. 7 40921 2017.
ISSN: ESSN 2045-2322
PubMed: 28098230
DOI: 10.1038/SREP40921