Magnesium in PDB 6qzg: Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta- Phosphoglucomutse in An Open Conformation.

All present enzymatic activity of Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta- Phosphoglucomutse in An Open Conformation.:
5.4.2.6;

The structure of Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta- Phosphoglucomutse in An Open Conformation., PDB code: 6qzg was solved by A.J.Robertson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.66 / 2.47
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.270, 117.330, 52.780, 90.00, 97.78, 90.00
R / Rfree (%)	19.3 / 27.8

The binding sites of Magnesium atom in the Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta- Phosphoglucomutse in An Open Conformation. (pdb code 6qzg). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta- Phosphoglucomutse in An Open Conformation., PDB code: 6qzg:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta- Phosphoglucomutse in An Open Conformation.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta- Phosphoglucomutse in An Open Conformation. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:27.7 occ:1.00 O A:ASP10 2.1 33.6 1.0 OD2 A:ASP8 2.1 39.1 1.0 O A:HOH423 2.1 31.3 1.0 O17 A:JLT302 2.2 57.1 1.0 OD1 A:ASP170 2.2 35.9 1.0 O A:HOH432 2.2 31.3 1.0 CG A:ASP8 2.8 36.2 1.0 OD1 A:ASP8 2.9 37.9 1.0 C A:ASP10 3.2 32.1 1.0 CG A:ASP170 3.2 36.5 1.0 P11 A:JLT302 3.6 71.0 1.0 OD2 A:ASP170 3.7 35.3 1.0 OE1 A:GLU169 3.9 49.0 1.0 O18 A:JLT302 3.9 57.4 1.0 O3 A:JLT302 4.0 60.2 1.0 CA A:ASP10 4.0 30.9 1.0 CB A:ASP10 4.0 31.2 1.0 N A:ASP10 4.2 31.3 1.0 CB A:ASP8 4.2 32.1 1.0 N A:GLY11 4.2 33.9 1.0 O16 A:JLT302 4.3 54.0 1.0 OD2 A:ASP10 4.3 38.7 1.0 OE2 A:GLU169 4.4 57.4 1.0 CD A:GLU169 4.5 51.0 1.0 CB A:ASP170 4.5 30.8 1.0 CA A:GLY11 4.5 30.7 1.0 CG A:ASP10 4.6 33.1 1.0 N A:ASP170 4.7 34.5 1.0 C A:LEU9 4.9 29.2 1.0 N A:LEU9 5.0 29.9 1.0

Magnesium binding site 2 out of 2 in the Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta- Phosphoglucomutse in An Open Conformation.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta- Phosphoglucomutse in An Open Conformation. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:27.7 occ:1.00 O B:HOH405 1.8 34.9 1.0 OD2 B:ASP8 1.9 39.3 1.0 O B:HOH429 2.2 26.3 1.0 O B:ASP10 2.3 39.4 1.0 OD1 B:ASP170 2.3 36.2 1.0 O16 B:JLT302 2.4 48.9 0.5 O16 B:JLT302 2.5 59.7 0.5 CG B:ASP8 2.8 41.6 1.0 OE2 B:GLU169 3.0 61.8 1.0 OD1 B:ASP8 3.2 38.4 1.0 CG B:ASP170 3.4 33.6 1.0 C B:ASP10 3.5 32.9 1.0 OD2 B:ASP170 3.7 30.8 1.0 P11 B:JLT302 3.9 55.5 0.5 O3 B:JLT302 3.9 53.4 0.5 P11 B:JLT302 4.0 67.9 0.5 CD B:GLU169 4.1 50.2 1.0 CB B:ASP10 4.2 32.7 1.0 CB B:ASP8 4.2 37.6 1.0 CA B:ASP10 4.2 34.5 1.0 OD2 B:ASP10 4.3 34.6 1.0 O3 B:JLT302 4.4 67.3 0.5 N B:ASP10 4.4 33.1 1.0 OE1 B:GLU169 4.5 46.9 1.0 O17 B:JLT302 4.5 51.2 0.5 N B:GLY11 4.5 31.3 1.0 O18 B:JLT302 4.5 51.7 0.5 O B:HOH456 4.5 47.7 1.0 O17 B:JLT302 4.5 61.3 0.5 OG B:SER171 4.6 40.5 1.0 CG B:ASP10 4.6 35.6 1.0 O18 B:JLT302 4.7 63.2 0.5 CB B:ASP170 4.7 37.0 1.0 N B:ASP170 4.7 36.8 1.0 CA B:GLY11 4.7 31.8 1.0 CB B:SER171 4.8 37.1 1.0 N B:SER171 5.0 33.1 1.0

A.J.Robertson, J.P.Waltho. Beta-Glucose 1,6-Bisphosphonate Bound to Wild Type Beta-Phosphoglucomutse in An Open Conformation. To Be Published.