Magnesium in PDB 4u94: Structure of Mycobacterial Maltokinase, the Missing Link in the Essential Glge-Pathway

All present enzymatic activity of Structure of Mycobacterial Maltokinase, the Missing Link in the Essential Glge-Pathway:
2.7.1.175;

The structure of Structure of Mycobacterial Maltokinase, the Missing Link in the Essential Glge-Pathway, PDB code: 4u94 was solved by J.Fraga, N.Empadinhas, P.J.B.Pereira, S.Macedo-Ribeiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.74 / 1.47
Space group	P 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	62.947, 73.409, 106.890, 90.00, 90.00, 90.00
R / Rfree (%)	14 / 18

The binding sites of Magnesium atom in the Structure of Mycobacterial Maltokinase, the Missing Link in the Essential Glge-Pathway (pdb code 4u94). 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 Mycobacterial Maltokinase, the Missing Link in the Essential Glge-Pathway, PDB code: 4u94:

Magnesium binding site 1 out of 1 in the Structure of Mycobacterial Maltokinase, the Missing Link in the Essential Glge-Pathway


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Mycobacterial Maltokinase, the Missing Link in the Essential Glge-Pathway within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:30.0 occ:0.62 O A:HOH1173 2.1 44.5 1.0 OE1 A:GLN310 2.4 17.7 1.0 OD2 A:ASP322 2.4 28.6 1.0 CG A:ASP322 3.3 23.1 1.0 CD A:GLN310 3.4 13.2 1.0 CB A:ASP322 3.6 15.5 1.0 NE2 A:GLN310 3.8 14.4 1.0 O A:HOH1080 3.9 41.3 1.0 O A:HOH965 3.9 31.7 1.0 OD1 A:ASP322 4.5 23.6 1.0 O A:GLY309 4.5 15.2 1.0 CG A:GLN310 4.7 12.7 1.0 O A:HOH903 4.8 24.6 1.0

J.Fraga, A.Maranha, V.Mendes, P.J.Pereira, N.Empadinhas, S.Macedo-Ribeiro. Structure of Mycobacterial Maltokinase, the Missing Link in the Essential Glge-Pathway. Sci Rep V. 5 8026 2015.
ISSN: ESSN 2045-2322
PubMed: 25619172
DOI: 10.1038/SREP08026