Magnesium in PDB 6hdh: R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A.

All present enzymatic activity of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A.:
5.4.2.6;

The structure of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A., PDB code: 6hdh 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)	31.36 / 1.62
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.130, 117.230, 53.010, 90.00, 97.41, 90.00
R / Rfree (%)	18.2 / 21.8

The binding sites of Magnesium atom in the R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A. (pdb code 6hdh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A., PDB code: 6hdh:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:26.6 occ:1.00 OD1 A:ASP170 2.2 27.9 1.0 OD2 A:ASP8 2.2 27.5 1.0 O A:HOH487 2.3 31.7 1.0 O A:ASP10 2.3 25.4 1.0 OE1 A:GLU169 2.6 27.5 1.0 CG A:ASP8 3.3 25.5 1.0 CG A:ASP170 3.4 29.1 1.0 O A:HOH438 3.4 32.6 1.0 C A:ASP10 3.5 22.9 1.0 CD A:GLU169 3.5 28.0 1.0 CB A:ASP8 3.8 24.9 1.0 O A:HOH412 3.9 27.9 1.0 OE2 A:GLU169 3.9 25.2 1.0 OD2 A:ASP170 4.0 28.2 1.0 N A:ASP170 4.1 22.5 1.0 O A:HOH426 4.4 34.7 1.0 OD1 A:ASP8 4.4 23.9 1.0 N A:GLY11 4.4 22.8 1.0 CB A:ASP170 4.4 25.8 1.0 CA A:GLY11 4.4 24.0 1.0 CA A:ASP10 4.5 22.2 1.0 CB A:ASP10 4.6 26.0 1.0 OG A:SER171 4.6 28.3 1.0 CG2 A:VAL12 4.6 23.1 1.0 N A:ASP10 4.6 21.8 1.0 N A:SER171 4.7 25.5 1.0 CB A:SER171 4.7 28.3 1.0 CA A:ASP170 4.7 24.3 1.0 CG A:GLU169 4.8 25.6 1.0 C A:GLY11 4.8 23.4 1.0 CA A:GLU169 4.9 22.5 1.0 C A:ASP170 5.0 27.3 1.0

Magnesium binding site 2 out of 2 in the R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 1.6 A. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:28.8 occ:1.00 OD1 B:ASP170 2.2 28.9 1.0 OD2 B:ASP8 2.2 26.7 1.0 O B:HOH484 2.2 37.5 1.0 O B:ASP10 2.4 26.1 1.0 OE1 B:GLU169 2.6 27.5 1.0 CG B:ASP8 3.3 24.3 1.0 O B:HOH430 3.3 31.9 1.0 CG B:ASP170 3.4 30.2 1.0 CD B:GLU169 3.5 24.1 1.0 C B:ASP10 3.6 24.5 1.0 CB B:ASP8 3.8 22.1 1.0 OE2 B:GLU169 3.9 26.1 1.0 N B:ASP170 4.0 23.1 1.0 OD2 B:ASP170 4.1 30.0 1.0 OD1 B:ASP8 4.4 24.9 1.0 O B:HOH473 4.4 42.1 1.0 CB B:ASP170 4.4 25.5 1.0 N B:GLY11 4.5 22.6 1.0 CA B:ASP10 4.5 24.1 1.0 CA B:GLY11 4.5 22.6 1.0 OG B:SER171 4.6 25.3 1.0 CG2 B:VAL12 4.6 23.4 1.0 N B:SER171 4.6 22.8 1.0 N B:ASP10 4.6 23.3 1.0 CB B:SER171 4.6 24.9 1.0 CB B:ASP10 4.6 26.4 1.0 CA B:ASP170 4.7 22.4 1.0 CG B:GLU169 4.8 21.8 1.0 C B:ASP170 4.9 25.4 1.0 CA B:GLU169 4.9 20.2 1.0 C B:GLY11 4.9 23.4 1.0 C B:GLU169 5.0 22.9 1.0

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