Magnesium in PDB 7oml: Bacillus Subtilis Phosphoglucomutase Glmm (Metal Bound)

All present enzymatic activity of Bacillus Subtilis Phosphoglucomutase Glmm (Metal Bound):
5.4.2.10;

The structure of Bacillus Subtilis Phosphoglucomutase Glmm (Metal Bound), PDB code: 7oml was solved by M.Pathania, A.G.Grundling, P.Freemont, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.15 / 2.90
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	134.418, 134.418, 69.012, 90, 90, 120
R / Rfree (%)	19 / 23.4

The binding sites of Magnesium atom in the Bacillus Subtilis Phosphoglucomutase Glmm (Metal Bound) (pdb code 7oml). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Bacillus Subtilis Phosphoglucomutase Glmm (Metal Bound), PDB code: 7oml:

Magnesium binding site 1 out of 1 in the Bacillus Subtilis Phosphoglucomutase Glmm (Metal Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bacillus Subtilis Phosphoglucomutase Glmm (Metal Bound) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:34.0 occ:1.00 OG A:SER100 1.8 40.3 1.0 OD2 A:ASP244 2.1 35.6 1.0 O A:HOH601 2.4 43.4 1.0 O A:HOH602 2.4 40.5 1.0 OD2 A:ASP240 2.4 44.6 1.0 OD2 A:ASP242 2.4 37.6 1.0 CG A:ASP244 3.1 44.9 1.0 CB A:SER100 3.1 49.8 1.0 CG A:ASP242 3.2 35.3 1.0 OD1 A:ASP242 3.2 39.8 1.0 OD1 A:ASP244 3.4 50.5 1.0 CG A:ASP240 3.4 37.6 1.0 OD1 A:ASP240 3.8 34.3 1.0 CA A:SER100 3.8 32.6 1.0 CD2 A:HIS101 4.2 37.8 1.0 CB A:ASP244 4.4 27.1 1.0 NE A:ARG245 4.5 34.6 1.0 C A:SER100 4.5 34.1 1.0 CB A:ASP242 4.7 26.3 1.0 N A:HIS101 4.7 36.7 1.0 CB A:ASP240 4.7 29.6 1.0 CG A:ARG245 4.7 21.7 1.0 N A:ASP244 4.8 26.5 1.0 N A:ASP242 4.9 30.3 1.0 NE2 A:HIS101 4.9 48.2 1.0 N A:ARG245 5.0 29.2 1.0 CD A:ARG245 5.0 33.6 1.0 N A:SER100 5.0 37.3 1.0

M.Pathania, A.G.Grundling, P.Freemont. Complex Structure of the Bacillus Subtilis Cdaa C-Di-Amp Cyclase Domain and the Phosphoglucomutase Glmm To Be Published.