Magnesium in PDB 6h93: Beta-Phosphoglucomutase From Lactococcus Lactis with Inorganic Phosphate Bound in An Open Conformer to 1.8 A.

All present enzymatic activity of Beta-Phosphoglucomutase From Lactococcus Lactis with Inorganic Phosphate Bound in An Open Conformer to 1.8 A.:
5.4.2.6;

The structure of Beta-Phosphoglucomutase From Lactococcus Lactis with Inorganic Phosphate Bound in An Open Conformer to 1.8 A., PDB code: 6h93 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)	32.05 / 1.77
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.350, 117.140, 53.190, 90.00, 99.14, 90.00
R / Rfree (%)	17.9 / 23.3

The binding sites of Magnesium atom in the Beta-Phosphoglucomutase From Lactococcus Lactis with Inorganic Phosphate Bound in An Open Conformer to 1.8 A. (pdb code 6h93). 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-Phosphoglucomutase From Lactococcus Lactis with Inorganic Phosphate Bound in An Open Conformer to 1.8 A., PDB code: 6h93:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Beta-Phosphoglucomutase From Lactococcus Lactis with Inorganic Phosphate Bound in An Open Conformer to 1.8 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 with Inorganic Phosphate Bound in An Open Conformer to 1.8 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:26.6 occ:1.00 OD1 A:ASP170 2.1 25.3 1.0 O A:HOH523 2.2 31.4 1.0 O A:ASP10 2.2 22.0 1.0 OD2 A:ASP8 2.2 24.3 1.0 OE1 A:GLU169 2.7 22.8 1.0 CG A:ASP8 3.3 24.0 1.0 CG A:ASP170 3.3 28.9 1.0 C A:ASP10 3.4 21.7 1.0 CD A:GLU169 3.6 24.0 1.0 O A:HOH430 3.6 31.2 1.0 CB A:ASP8 3.7 21.6 1.0 O A:HOH415 3.8 25.1 1.0 OE2 A:GLU169 3.9 23.6 1.0 OD2 A:ASP170 4.0 27.9 1.0 N A:ASP170 4.1 22.7 1.0 O A:HOH521 4.1 43.5 1.0 N A:GLY11 4.3 22.2 1.0 OD1 A:ASP8 4.4 24.8 1.0 CA A:GLY11 4.4 23.3 1.0 CA A:ASP10 4.4 22.1 1.0 CB A:ASP170 4.4 25.1 1.0 CB A:ASP10 4.5 23.2 1.0 CG2 A:VAL12 4.5 23.4 1.0 O A:HOH459 4.6 32.4 1.0 N A:ASP10 4.6 21.0 1.0 N A:SER171 4.6 26.1 1.0 CA A:ASP170 4.7 24.9 1.0 OG A:SER171 4.7 26.2 1.0 C A:GLY11 4.7 22.2 1.0 CB A:SER171 4.7 26.3 1.0 CG A:GLU169 4.8 21.7 1.0 N A:VAL12 4.9 22.1 1.0 CA A:GLU169 5.0 20.8 1.0 C A:ASP170 5.0 27.7 1.0

Magnesium binding site 2 out of 2 in the Beta-Phosphoglucomutase From Lactococcus Lactis with Inorganic Phosphate Bound in An Open Conformer to 1.8 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Beta-Phosphoglucomutase From Lactococcus Lactis with Inorganic Phosphate Bound in An Open Conformer to 1.8 A. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:34.3 occ:1.00 O B:HOH508 1.9 46.1 1.0 OD1 B:ASP170 2.1 29.8 1.0 OD2 B:ASP8 2.2 28.2 1.0 O B:ASP10 2.2 25.3 1.0 OE1 B:GLU169 2.8 29.7 1.0 O B:HOH442 3.2 32.2 1.0 CG B:ASP170 3.3 30.3 1.0 CG B:ASP8 3.3 26.6 1.0 C B:ASP10 3.4 24.6 1.0 O B:HOH406 3.6 37.2 1.0 CD B:GLU169 3.7 27.4 1.0 CB B:ASP8 3.9 24.5 1.0 OD2 B:ASP170 3.9 31.1 1.0 OE2 B:GLU169 4.0 27.7 1.0 N B:ASP170 4.1 26.5 1.0 OD1 B:ASP8 4.3 26.0 1.0 O B:HOH490 4.3 46.6 1.0 CA B:ASP10 4.3 24.9 1.0 CB B:ASP170 4.4 27.5 1.0 N B:GLY11 4.4 25.7 1.0 CA B:GLY11 4.5 24.3 1.0 CB B:ASP10 4.5 25.7 1.0 OG B:SER171 4.6 28.9 1.0 N B:ASP10 4.6 22.5 1.0 CG2 B:VAL12 4.6 23.5 1.0 N B:SER171 4.7 28.4 1.0 CA B:ASP170 4.7 27.3 1.0 CB B:SER171 4.7 29.0 1.0 C B:GLY11 4.9 25.1 1.0 C B:ASP170 4.9 27.9 1.0 OD2 B:ASP10 5.0 30.6 1.0 CG B:GLU169 5.0 26.6 1.0

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