Magnesium in PDB 6h91: Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A

All present enzymatic activity of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A:
5.4.2.6;

The structure of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A, PDB code: 6h91 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)	58.62 / 2.38
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.330, 117.230, 52.930, 90.00, 97.75, 90.00
R / Rfree (%)	21.9 / 29.9

The binding sites of Magnesium atom in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A (pdb code 6h91). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A, PDB code: 6h91:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:26.9 occ:1.00 O A:HOH410 1.9 16.8 1.0 O A:HOH412 2.0 30.3 1.0 OP1 A:PHD8 2.0 26.1 1.0 OD1 A:ASP170 2.1 31.2 1.0 O A:ASP10 2.2 32.8 1.0 OD2 A:PHD8 2.2 27.4 1.0 CG A:ASP170 3.1 33.2 1.0 CG A:PHD8 3.1 28.1 1.0 C A:ASP10 3.3 32.0 1.0 P A:PHD8 3.3 26.6 1.0 OD2 A:ASP170 3.3 29.9 1.0 OD1 A:PHD8 3.5 27.7 1.0 OE1 A:GLU169 3.9 37.6 1.0 O A:HOH411 4.0 29.8 1.0 CB A:ASP10 4.0 29.9 1.0 CA A:ASP10 4.0 30.3 1.0 OD2 A:ASP10 4.1 32.5 1.0 OP2 A:PHD8 4.2 26.7 1.0 OP3 A:PHD8 4.3 27.5 1.0 N A:ASP10 4.3 29.8 1.0 N A:GLY11 4.3 34.5 1.0 CG A:ASP10 4.3 29.8 1.0 CB A:ASP170 4.4 32.8 1.0 CB A:PHD8 4.4 27.9 1.0 CA A:GLY11 4.5 33.8 1.0 N A:ASP170 4.6 35.8 1.0 CD A:GLU169 4.7 39.0 1.0 OE2 A:GLU169 4.9 41.4 1.0 C A:LEU9 5.0 28.3 1.0

Magnesium binding site 2 out of 2 in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.4 A within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:28.6 occ:1.00 O B:HOH416 2.0 22.9 1.0 OD1 B:ASP170 2.0 31.3 1.0 OD2 B:PHD8 2.0 24.0 1.0 O B:HOH413 2.1 26.7 1.0 O B:ASP10 2.1 30.6 1.0 OP2 B:PHD8 2.1 22.1 1.0 CG B:ASP170 3.0 31.9 1.0 CG B:PHD8 3.1 24.4 1.0 C B:ASP10 3.3 30.9 1.0 OD2 B:ASP170 3.4 31.2 1.0 P B:PHD8 3.4 24.1 1.0 OD1 B:PHD8 3.5 23.2 1.0 OE1 B:GLU169 3.9 33.9 1.0 CB B:ASP10 4.0 31.6 1.0 CA B:ASP10 4.1 30.2 1.0 OP1 B:PHD8 4.2 24.1 1.0 OD2 B:ASP10 4.2 36.1 1.0 N B:GLY11 4.3 29.4 1.0 N B:ASP10 4.3 29.6 1.0 CB B:ASP170 4.3 32.7 1.0 CB B:PHD8 4.4 25.6 1.0 OP3 B:PHD8 4.4 22.8 1.0 CG B:ASP10 4.4 34.9 1.0 O B:HOH404 4.4 32.1 1.0 N B:ASP170 4.5 31.5 1.0 CA B:GLY11 4.5 28.1 1.0 CD B:GLU169 4.6 32.5 1.0 OE2 B:GLU169 4.8 30.6 1.0 CA B:ASP170 4.8 32.0 1.0 C B:LEU9 4.9 28.5 1.0 OG B:SER171 5.0 28.0 1.0 CB B:SER171 5.0 27.2 1.0 N B:SER171 5.0 30.0 1.0

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