Magnesium in PDB 4ajs: 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II), Adenosine 2',5'-Biphosphate and Ribosylnicotinamide-5'-Phosphate

The structure of 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II), Adenosine 2',5'-Biphosphate and Ribosylnicotinamide-5'-Phosphate, PDB code: 4ajs was solved by S.Goncalves, S.P.Miller, M.A.Carrondo, A.M.Dean, P.M.Matias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.325 / 1.80
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	103.585, 103.585, 149.680, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 19.19

The binding sites of Magnesium atom in the 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II), Adenosine 2',5'-Biphosphate and Ribosylnicotinamide-5'-Phosphate (pdb code 4ajs). 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 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II), Adenosine 2',5'-Biphosphate and Ribosylnicotinamide-5'-Phosphate, PDB code: 4ajs:

Magnesium binding site 1 out of 1 in the 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II), Adenosine 2',5'-Biphosphate and Ribosylnicotinamide-5'-Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 3D Structure of E. Coli Isocitrate Dehydrogenase K100M Mutant in Complex with Isocitrate, Magnesium(II), Adenosine 2',5'-Biphosphate and Ribosylnicotinamide-5'-Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:24.1 occ:1.00 OD1 A:ASP307 2.1 20.8 1.0 O A:HOH2208 2.1 22.1 1.0 O2 A:ICT502 2.2 20.9 0.9 O A:HOH2410 2.2 25.2 1.0 O7 A:ICT502 2.2 22.1 0.9 C1 A:ICT502 3.0 25.6 0.9 C2 A:ICT502 3.1 22.0 0.9 CG A:ASP307 3.2 23.0 1.0 OD2 A:ASP307 3.7 22.0 1.0 OD1 A:ASP311 4.0 27.1 1.0 O A:HOH2209 4.0 28.2 0.5 C6 A:ICT502 4.1 23.3 0.9 O A:ASP307 4.1 20.1 1.0 O1 A:ICT502 4.2 26.4 0.9 O A:HOH2412 4.2 25.8 0.8 C3 A:ICT502 4.2 23.9 0.9 NH1 A:ARG129 4.3 23.9 1.0 O6 A:ICT502 4.3 23.8 0.9 O A:HOH2499 4.3 29.5 0.8 OD2 A:ASP311 4.3 27.9 1.0 CG A:ASP311 4.3 26.6 1.0 CB A:ASP307 4.4 19.3 1.0 O5 A:ICT502 4.4 24.2 0.9 CA A:ASP307 4.5 18.0 1.0 O A:HOH2427 4.6 30.8 0.5 C A:ASP307 4.6 22.8 1.0 NH1 A:ARG153 4.7 21.4 1.0

S.Goncalves, S.P.Miller, M.A.Carrondo, A.M.Dean, P.M.Matias. Induced Fit and the Catalytic Mechanism of Isocitrate Dehydrogenase. Biochemistry V. 51 7098 2012.
ISSN: ISSN 0006-2960
PubMed: 22891681
DOI: 10.1021/BI300483W