Magnesium in PDB 6ydk: Substrate-Free P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis

All present enzymatic activity of Substrate-Free P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis:
5.4.2.6;

The structure of Substrate-Free P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis, PDB code: 6ydk was solved by H.P.Wood, F.A.Cruz-Navarrete, N.J.Baxter, C.R.Trevitt, A.J.Robertson, S.R.Dix, A.M.Hounslow, M.J.Cliff, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.95 / 2.02
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.300, 56.240, 77.660, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 25.1

The binding sites of Magnesium atom in the Substrate-Free P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis (pdb code 6ydk). 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 Substrate-Free P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis, PDB code: 6ydk:

Magnesium binding site 1 out of 1 in the Substrate-Free P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Substrate-Free P146A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:45.5 occ:1.00 OD2 A:ASP8 1.9 46.6 1.0 O A:ASP10 2.0 33.7 1.0 O A:HOH410 2.1 41.3 1.0 OD1 A:ASP170 2.2 36.3 1.0 O A:HOH422 2.2 46.8 1.0 O A:HOH419 2.2 39.9 1.0 CG A:ASP8 3.1 39.1 1.0 C A:ASP10 3.2 35.1 1.0 CG A:ASP170 3.2 38.4 1.0 OD2 A:ASP170 3.6 43.6 1.0 OD1 A:ASP8 3.6 40.3 1.0 OE1 A:GLU169 3.7 47.0 1.0 CA A:ASP10 4.1 35.4 1.0 N A:GLY11 4.1 34.8 1.0 CB A:ASP8 4.2 36.5 1.0 CB A:ASP10 4.2 36.5 1.0 CA A:GLY11 4.3 34.6 1.0 OD2 A:ASP10 4.3 43.7 1.0 N A:ASP10 4.3 32.8 1.0 CD A:GLU169 4.4 43.4 1.0 CB A:ASP170 4.5 38.5 1.0 N A:ASP170 4.5 34.5 1.0 OE2 A:GLU169 4.6 43.1 1.0 CG A:ASP10 4.7 41.0 1.0 C A:GLY11 4.9 34.0 1.0 O A:HOH402 4.9 32.0 1.0 CG2 A:VAL12 4.9 35.1 1.0 CA A:ASP170 5.0 39.5 1.0

H.P.Wood, F.A.Cruz-Navarrete, N.J.Baxter, C.R.Trevitt, A.J.Robertson, S.R.Dix, A.M.Hounslow, M.J.Cliff, J.P.Waltho. Allomorphy As A Mechanism of Post-Translational Control of Enzyme Activity. Nat Commun V. 11 5538 2020.
ISSN: ESSN 2041-1723
PubMed: 33139716
DOI: 10.1038/S41467-020-19215-9