Magnesium in PDB 6hdi: R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.0 A.

All present enzymatic activity of R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.0 A.:
5.4.2.6;

The structure of R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.0 A., PDB code: 6hdi 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)	52.64 / 2.03
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.200, 116.900, 53.170, 90.00, 98.09, 90.00
R / Rfree (%)	20.5 / 27.3

The binding sites of Magnesium atom in the R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.0 A. (pdb code 6hdi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.0 A., PDB code: 6hdi:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.0 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.0 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:20.6 occ:1.00 O A:HOH484 2.1 33.9 1.0 OD2 A:ASP8 2.1 26.0 1.0 OD1 A:ASP170 2.2 25.8 1.0 O A:ASP10 2.4 21.3 1.0 OE1 A:GLU169 2.6 26.5 1.0 O A:HOH432 3.0 29.8 1.0 CG A:ASP8 3.2 21.0 1.0 CG A:ASP170 3.3 27.3 1.0 CD A:GLU169 3.5 23.2 1.0 C A:ASP10 3.5 19.3 1.0 OE2 A:GLU169 3.7 25.0 1.0 CB A:ASP8 3.7 22.1 1.0 O A:HOH427 3.7 32.4 1.0 OD2 A:ASP170 3.9 25.7 1.0 N A:ASP170 4.2 22.5 1.0 OD1 A:ASP8 4.2 20.1 1.0 O A:HOH412 4.2 29.6 1.0 CA A:ASP10 4.4 20.3 1.0 N A:GLY11 4.4 22.0 1.0 CB A:ASP170 4.5 24.6 1.0 CG2 A:VAL12 4.5 24.4 1.0 CA A:GLY11 4.5 20.9 1.0 CB A:ASP10 4.6 22.3 1.0 N A:ASP10 4.6 20.7 1.0 N A:SER171 4.7 26.7 1.0 CB A:SER171 4.7 26.5 1.0 OG A:SER171 4.7 27.6 1.0 CA A:ASP170 4.8 25.4 1.0 CG A:GLU169 4.8 21.9 1.0 OD2 A:ASP10 4.8 23.0 1.0 C A:ASP170 4.9 24.9 1.0 C A:GLY11 5.0 22.3 1.0

Magnesium binding site 2 out of 2 in the R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.0 A.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of R49A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.0 A. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:25.9 occ:1.00 OD2 B:ASP8 2.1 26.0 1.0 OD1 B:ASP170 2.2 22.5 1.0 O B:ASP10 2.3 22.6 1.0 OE1 B:GLU169 2.7 25.4 1.0 O B:HOH444 3.2 28.5 1.0 CG B:ASP8 3.2 22.6 1.0 CG B:ASP170 3.4 21.7 1.0 C B:ASP10 3.5 21.2 1.0 CD B:GLU169 3.6 26.2 1.0 CB B:ASP8 3.7 20.3 1.0 OE2 B:GLU169 3.9 24.4 1.0 OD2 B:ASP170 4.0 21.6 1.0 N B:ASP170 4.1 25.1 1.0 OD1 B:ASP8 4.2 21.8 1.0 CG2 B:VAL12 4.3 20.7 1.0 CA B:ASP10 4.4 20.9 1.0 CB B:ASP10 4.4 22.4 1.0 N B:GLY11 4.5 22.4 1.0 N B:ASP10 4.5 18.5 1.0 CB B:ASP170 4.5 21.6 1.0 CA B:GLY11 4.6 20.7 1.0 OG B:SER171 4.6 20.5 1.0 CA B:ASP170 4.8 23.4 1.0 N B:SER171 4.8 23.5 1.0 CG B:GLU169 4.8 25.5 1.0 C B:GLY11 4.8 21.5 1.0 CB B:SER171 4.9 21.0 1.0 N B:VAL12 4.9 20.3 1.0 CA B:GLU169 4.9 22.1 1.0 O B:HOH441 4.9 30.3 1.0 OD2 B:ASP10 4.9 25.5 1.0 CG B:ASP10 5.0 26.4 1.0 C B:ASP170 5.0 23.9 1.0

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