Magnesium in PDB 6uiq: Crystal Structure of Wild-Type Human Phosphoglucomutase 1 in Complex with Glucose-6-Phosphate

All present enzymatic activity of Crystal Structure of Wild-Type Human Phosphoglucomutase 1 in Complex with Glucose-6-Phosphate:
5.4.2.2;

The structure of Crystal Structure of Wild-Type Human Phosphoglucomutase 1 in Complex with Glucose-6-Phosphate, PDB code: 6uiq was solved by K.M.Stiers, L.J.Beamer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.81 / 2.30
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	171.874, 171.874, 99.447, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 22.3

The binding sites of Magnesium atom in the Crystal Structure of Wild-Type Human Phosphoglucomutase 1 in Complex with Glucose-6-Phosphate (pdb code 6uiq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Wild-Type Human Phosphoglucomutase 1 in Complex with Glucose-6-Phosphate, PDB code: 6uiq:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Wild-Type Human Phosphoglucomutase 1 in Complex with Glucose-6-Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Wild-Type Human Phosphoglucomutase 1 in Complex with Glucose-6-Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg602 b:22.3 occ:1.00 OD1 B:ASP292 1.9 29.1 1.0 OD2 B:ASP288 1.9 31.6 1.0 OG B:SER117 2.1 29.7 1.0 O B:HOH735 2.2 26.9 1.0 OD1 B:ASP290 2.2 28.2 1.0 O B:HOH826 2.2 36.4 1.0 CG B:ASP292 3.0 30.0 1.0 CG B:ASP288 3.1 29.0 1.0 CG B:ASP290 3.1 28.9 1.0 OD2 B:ASP290 3.4 28.7 1.0 CB B:SER117 3.4 26.8 1.0 OD2 B:ASP292 3.5 32.9 1.0 OD1 B:ASP288 3.6 29.0 1.0 CA B:SER117 4.0 31.4 1.0 CD B:ARG293 4.1 38.0 1.0 N B:ASP292 4.2 30.8 1.0 CB B:ASP288 4.3 22.9 1.0 CB B:ASP292 4.3 29.9 1.0 CB B:ASP290 4.5 27.7 1.0 ND1 B:HIS118 4.5 47.5 1.0 C B:SER117 4.5 30.6 1.0 N B:HIS118 4.7 30.2 1.0 N B:ASP290 4.7 31.4 1.0 CA B:ASP292 4.7 23.5 1.0 N B:ARG293 4.7 25.1 1.0 CG B:ARG293 4.7 39.0 1.0 N B:GLY291 4.8 31.4 1.0 CB B:ARG293 4.8 26.4 1.0 C B:ASP292 4.8 26.8 1.0 CA B:ASP290 5.0 31.0 1.0 C B:ASP290 5.0 29.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Wild-Type Human Phosphoglucomutase 1 in Complex with Glucose-6-Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Wild-Type Human Phosphoglucomutase 1 in Complex with Glucose-6-Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:35.9 occ:1.00 OD2 A:ASP288 2.0 48.9 1.0 O A:HOH737 2.0 36.9 1.0 OD1 A:ASP292 2.1 45.1 1.0 OG A:SER117 2.2 39.3 1.0 O A:HOH856 2.3 31.6 1.0 OD1 A:ASP290 2.4 43.5 1.0 CG A:ASP292 3.1 36.5 1.0 CG A:ASP288 3.1 40.7 1.0 CB A:SER117 3.2 34.4 1.0 CG A:ASP290 3.3 44.6 1.0 OD2 A:ASP292 3.4 40.9 1.0 OD2 A:ASP290 3.5 40.4 1.0 CD A:ARG293 3.7 47.3 1.0 OD1 A:ASP288 3.7 43.3 1.0 CA A:SER117 4.0 36.9 1.0 ND1 A:HIS118 4.3 45.8 1.0 CB A:ASP288 4.3 28.7 1.0 CG A:ARG293 4.4 47.2 1.0 N A:HIS118 4.4 37.0 1.0 C A:SER117 4.5 37.2 1.0 CB A:ASP292 4.5 30.9 1.0 N A:ASP292 4.5 33.7 1.0 N A:ARG293 4.7 28.6 1.0 CB A:ASP290 4.7 42.8 1.0 CA A:ASP292 4.8 31.5 1.0 C A:ASP292 4.9 33.0 1.0 NE A:ARG293 4.9 50.3 1.0 N A:ASP290 4.9 35.1 1.0 CB A:ARG293 5.0 41.0 1.0

K.M.Stiers, L.J.Beamer. A Hotspot For Disease-Associated Variants of Human PGM1 Is Associated with Impaired Ligand Binding and Loop Dynamics. Structure V. 26 1337 2018.
ISSN: ISSN 1878-4186
PubMed: 30122451
DOI: 10.1016/J.STR.2018.07.005