Magnesium in PDB 1z4n: Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate Cocrystallized with Fluoride

All present enzymatic activity of Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate Cocrystallized with Fluoride:
5.4.2.6;

The structure of Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate Cocrystallized with Fluoride, PDB code: 1z4n was solved by L.W.Tremblay, G.Zhang, J.Dai, D.Dunaway-Mariano, K.N.Allen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 1.97
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.143, 36.451, 105.119, 90.00, 94.35, 90.00
R / Rfree (%)	20.7 / 23.9

The binding sites of Magnesium atom in the Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate Cocrystallized with Fluoride (pdb code 1z4n). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate Cocrystallized with Fluoride, PDB code: 1z4n:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate Cocrystallized with Fluoride


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate Cocrystallized with Fluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg800 b:16.6 occ:1.00 OD1 A:ASP170 2.3 12.3 1.0 OD2 A:ASP8 2.3 12.7 1.0 OE1 A:GLU169 2.4 13.6 1.0 O A:ASP10 2.4 15.1 1.0 O A:HOH1311 2.6 26.6 1.0 CD A:GLU169 3.4 12.4 1.0 CG A:ASP170 3.4 11.5 1.0 C A:ASP10 3.4 13.9 1.0 O A:HOH1286 3.4 17.3 1.0 CG A:ASP8 3.5 16.5 1.0 OE2 A:GLU169 3.7 12.7 1.0 N A:ASP170 3.9 13.3 1.0 O A:HOH1241 3.9 14.7 1.0 CB A:ASP8 4.0 14.4 1.0 CB A:ASP10 4.0 13.5 1.0 OD2 A:ASP170 4.1 12.1 1.0 CA A:ASP10 4.2 14.4 1.0 OD1 A:ASP10 4.2 15.0 1.0 CB A:ASP170 4.3 14.8 1.0 N A:GLY11 4.4 15.4 1.0 OG A:SER171 4.4 26.8 1.0 CG A:ASP10 4.4 15.3 1.0 N A:SER171 4.4 18.7 1.0 CA A:ASP170 4.5 15.9 1.0 OD1 A:ASP8 4.5 14.2 1.0 N A:ASP10 4.6 12.0 1.0 CA A:GLY11 4.6 13.3 1.0 CG A:GLU169 4.6 12.1 1.0 CB A:SER171 4.7 22.7 1.0 CA A:GLU169 4.8 12.4 1.0 C A:ASP170 4.8 17.0 1.0 C A:GLU169 4.8 13.4 1.0 CG2 A:VAL12 4.9 10.1 1.0 CE A:LYS45 4.9 41.8 1.0 CB A:GLU169 5.0 12.1 1.0

Magnesium binding site 2 out of 2 in the Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate Cocrystallized with Fluoride


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Beta-Phosphoglucomutase with Inhibitor Bound Alpha- Galactose 1-Phosphate Cocrystallized with Fluoride within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg801 b:27.9 occ:1.00 OD1 B:ASP170 2.3 37.8 1.0 OD2 B:ASP8 2.4 22.5 1.0 OE1 B:GLU169 2.5 27.0 1.0 O B:ASP10 2.5 32.9 1.0 O B:HOH1279 2.8 35.5 1.0 CD B:GLU169 3.3 27.2 1.0 O B:HOH1224 3.5 18.9 1.0 CG B:ASP170 3.5 35.8 1.0 CG B:ASP8 3.5 26.0 1.0 C B:ASP10 3.5 31.8 1.0 OE2 B:GLU169 3.7 25.4 1.0 N B:ASP170 3.7 32.1 1.0 CB B:ASP8 4.0 27.3 1.0 NZ B:LYS45 4.0 56.4 1.0 O B:HOH1237 4.0 34.4 1.0 CB B:ASP10 4.0 29.1 1.0 CA B:ASP10 4.2 30.7 1.0 OG B:SER171 4.2 39.7 1.0 CB B:ASP170 4.2 34.3 1.0 OD2 B:ASP170 4.3 36.0 1.0 CA B:ASP170 4.4 33.2 1.0 N B:SER171 4.4 34.0 1.0 OD2 B:ASP10 4.4 27.6 1.0 CG B:GLU169 4.5 27.9 1.0 N B:GLY11 4.5 33.1 1.0 OD1 B:ASP8 4.5 26.1 1.0 CG2 B:VAL12 4.5 31.1 1.0 N B:ASP10 4.6 28.6 1.0 CG B:ASP10 4.6 28.2 1.0 CA B:GLU169 4.6 30.8 1.0 C B:GLU169 4.7 32.0 1.0 C B:ASP170 4.7 33.5 1.0 CB B:SER171 4.7 37.5 1.0 CA B:GLY11 4.7 33.9 1.0 CB B:GLU169 4.8 30.2 1.0

L.W.Tremblay, G.Zhang, J.Dai, D.Dunaway-Mariano, K.N.Allen. Chemical Confirmation of A Pentavalent Phosphorane in Complex with Beta-Phosphoglucomutase J.Am.Chem.Soc. V. 127 5298 2005.
ISSN: ISSN 0002-7863
PubMed: 15826149
DOI: 10.1021/JA0509073