Magnesium in PDB 2b0t: Structure of Monomeric Nadp Isocitrate Dehydrogenase

All present enzymatic activity of Structure of Monomeric Nadp Isocitrate Dehydrogenase:
1.1.1.42;

The structure of Structure of Monomeric Nadp Isocitrate Dehydrogenase, PDB code: 2b0t was solved by F.Imabayashi, S.Aich, L.Prasad, L.T.Delbaere, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.75
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	129.046, 52.692, 124.035, 90.00, 108.98, 90.00
R / Rfree (%)	20 / 23

The binding sites of Magnesium atom in the Structure of Monomeric Nadp Isocitrate Dehydrogenase (pdb code 2b0t). 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 Structure of Monomeric Nadp Isocitrate Dehydrogenase, PDB code: 2b0t:

Magnesium binding site 1 out of 1 in the Structure of Monomeric Nadp Isocitrate Dehydrogenase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Monomeric Nadp Isocitrate Dehydrogenase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg800 b:16.6 occ:1.00 OD1 A:ASP548 2.1 23.9 1.0 OD2 A:ASP544 2.2 23.8 1.0 O A:ASP544 2.3 21.5 1.0 OD1 A:ASP346 2.3 33.2 1.0 O A:HOH936 2.3 27.3 1.0 O A:HOH831 2.3 23.7 1.0 CG A:ASP548 3.1 23.9 1.0 CG A:ASP544 3.2 23.8 1.0 C A:ASP544 3.2 20.7 1.0 CG A:ASP346 3.3 28.6 1.0 CA A:ASP544 3.7 20.3 1.0 OD2 A:ASP548 3.7 26.7 1.0 CB A:ASP346 3.8 26.3 1.0 CB A:ASP544 4.0 21.4 1.0 OD1 A:ASP544 4.0 25.1 1.0 O A:HOH958 4.0 33.0 1.0 CB A:ASP548 4.1 20.9 1.0 N A:TYR545 4.3 19.0 1.0 OD2 A:ASP346 4.3 30.2 1.0 O A:HOH1214 4.4 36.8 1.0 OG1 A:THR547 4.4 19.2 1.0 CA A:TYR545 4.7 19.0 1.0 N A:ASP548 4.9 20.3 1.0 NZ A:LYS253 4.9 38.2 1.0

F.Imabayashi, S.Aich, L.Prasad, L.T.Delbaere. Substrate-Free Structure of A Monomeric Nadp Isocitrate Dehydrogenase: An Open Conformation Phylogenetic Relationship of Isocitrate Dehydrogenase. Proteins V. 63 100 2006.
ISSN: ISSN 0887-3585
PubMed: 16416443
DOI: 10.1002/PROT.20867