Magnesium in PDB 6h8u: Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.9 A.

All present enzymatic activity of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.9 A.:
5.4.2.6;

The structure of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.9 A., PDB code: 6h8u was solved by A.J.Robertson, C.Bisson, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.45 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.150, 53.640, 81.070, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 23.9

The binding sites of Magnesium atom in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.9 A. (pdb code 6h8u). 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 Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.9 A., PDB code: 6h8u:

Magnesium binding site 1 out of 1 in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.9 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.9 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:27.5 occ:1.00 OD2 A:ASP8 1.8 28.9 1.0 OD1 A:ASP170 1.9 27.8 1.0 O A:HOH413 2.0 33.2 1.0 O A:HOH467 2.1 19.9 0.5 O A:ASP10 2.3 21.3 1.0 CG A:ASP8 3.1 25.5 1.0 CG A:ASP170 3.1 26.6 1.0 OE1 A:GLU169 3.1 30.8 1.0 C A:ASP10 3.5 23.0 1.0 OD2 A:ASP170 3.6 28.3 1.0 OD1 A:ASP8 3.8 26.3 1.0 CD A:GLU169 4.0 27.9 1.0 CB A:ASP8 4.1 24.4 1.0 N A:ASP170 4.2 25.1 1.0 CB A:ASP170 4.3 26.3 1.0 OE2 A:GLU169 4.3 23.4 1.0 N A:GLY11 4.3 21.7 1.0 CA A:ASP10 4.4 26.8 1.0 CA A:GLY11 4.4 22.3 1.0 CB A:ASP10 4.5 31.5 1.0 OD2 A:ASP10 4.6 37.1 1.0 N A:ASP10 4.6 26.0 1.0 N A:SER171 4.6 27.1 1.0 CA A:ASP170 4.7 26.7 1.0 CB A:SER171 4.7 26.8 1.0 OG A:SER171 4.8 27.0 1.0 C A:ASP170 4.8 25.9 1.0 C A:GLY11 4.9 23.1 1.0 CG2 A:VAL12 5.0 23.0 1.0

A.J.Robertson, C.Bisson, J.P.Waltho. Transition State of Phospho-Enzyme Hydrolysis in Beta-Phosphoglucomutase. To Be Published.