Magnesium in PDB 8q1e: D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate

The structure of D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate, PDB code: 8q1e was solved by F.A.Cruz-Navarrete, N.J.Baxter, A.J.Flinders, A.Buzoianu, M.J.Cliff, P.J.Baker, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.91 / 1.23
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	32.12, 83.757, 38.89, 90, 110.66, 90
R / Rfree (%)	15.2 / 19.4

The binding sites of Magnesium atom in the D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate (pdb code 8q1e). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate, PDB code: 8q1e:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:14.6 occ:1.00 O6P A:FBP301 2.0 14.6 1.0 OD2 A:ASP8 2.0 14.9 1.0 O A:ASN10 2.1 14.5 1.0 OD1 A:ASP170 2.1 14.9 1.0 O A:HOH419 2.1 14.6 1.0 O A:HOH427 2.1 16.3 1.0 CG A:ASP8 3.0 13.4 1.0 CG A:ASP170 3.0 15.5 1.0 C A:ASN10 3.2 13.3 1.0 OD1 A:ASP8 3.3 14.7 1.0 P2 A:FBP301 3.3 14.3 1.0 OD2 A:ASP170 3.5 18.6 1.0 MG A:MG303 3.7 14.2 1.0 O4P A:FBP301 3.9 15.3 1.0 CA A:ASN10 3.9 13.2 1.0 OE2 A:GLU169 3.9 16.9 1.0 N A:ASN10 3.9 13.1 1.0 O A:HOH510 4.0 35.5 1.0 CB A:ASN10 4.0 14.7 1.0 O5P A:FBP301 4.1 13.4 1.0 N A:GLY11 4.3 13.8 1.0 CB A:ASP170 4.3 14.4 1.0 CB A:ASP8 4.4 13.9 1.0 OE1 A:GLU169 4.4 14.6 1.0 CD A:GLU169 4.4 15.4 1.0 O6 A:FBP301 4.4 14.2 1.0 N A:ASP170 4.6 14.4 1.0 C6 A:FBP301 4.6 16.1 1.0 CA A:GLY11 4.7 14.9 1.0 O A:HOH475 4.7 21.6 1.0 C A:LEU9 4.7 12.8 1.0 O A:HOH491 4.9 17.9 1.0 CA A:ASP170 4.9 13.5 1.0

Magnesium binding site 2 out of 3 in the D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:14.2 occ:1.00 OD1 A:ASP8 2.0 14.7 1.0 O4P A:FBP301 2.0 15.3 1.0 O A:HOH491 2.1 17.9 1.0 O A:HOH444 2.1 14.8 1.0 OE1 A:GLU169 2.1 14.6 1.0 O A:HOH419 2.2 14.6 1.0 CG A:ASP8 2.9 13.4 1.0 P2 A:FBP301 3.1 14.3 1.0 CD A:GLU169 3.2 15.4 1.0 O6P A:FBP301 3.4 14.6 1.0 OD2 A:ASP8 3.4 14.9 1.0 OE2 A:GLU169 3.6 16.9 1.0 MG A:MG302 3.7 14.6 1.0 O A:HOH522 3.9 28.9 1.0 O A:HOH510 4.0 35.5 1.0 O5P A:FBP301 4.0 13.4 1.0 CB A:ASP8 4.1 13.9 1.0 N A:ALA115 4.2 14.7 1.0 O A:ALA113 4.4 15.9 1.0 O6 A:FBP301 4.4 14.2 1.0 CG A:GLU169 4.4 15.2 1.0 CB A:ALA115 4.5 16.6 1.0 CA A:SER114 4.7 14.9 1.0 C6 A:FBP301 4.7 16.1 1.0 CA A:ASP8 4.7 13.6 1.0 C A:SER114 4.9 15.3 1.0 O A:HOH506 4.9 26.1 1.0 OD1 A:ASP170 4.9 14.9 1.0 CZ A:PHE151 4.9 19.3 1.0 OG A:SER171 5.0 18.3 1.0 CA A:ALA115 5.0 15.0 1.0

Magnesium binding site 3 out of 3 in the D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of D10N,P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in Complex with Fructose 1,6-Bisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:52.6 occ:1.00 O A:HOH516 2.0 47.1 1.0 O A:HOH455 2.1 33.5 1.0 O A:HOH509 2.2 41.5 1.0 O A:HOH521 2.3 63.7 1.0 O A:HOH527 2.4 47.2 1.0 NE2 A:HIS206 2.6 30.7 1.0 CE1 A:HIS206 3.1 35.2 1.0 CD2 A:HIS206 3.9 28.1 1.0 O A:HOH409 4.0 34.7 1.0 ND1 A:HIS206 4.4 28.0 1.0 OD2 A:ASP203 4.7 20.8 1.0 CG A:HIS206 4.8 22.1 1.0 CG A:PRO202 4.8 24.3 1.0

F.A.Cruz-Navarrete, N.J.Baxter, A.J.Flinders, A.Buzoianu, M.J.Cliff, P.J.Baker, J.P.Waltho. Peri Active Site Catalysis of Proline Isomerisation Is the Molecular Basis of Allomorphy in Beta-Phosphoglucomutase. Commun Biol V. 7 909 2024.
ISSN: ESSN 2399-3642
PubMed: 39068257
DOI: 10.1038/S42003-024-06577-9