Magnesium in PDB 5epc: Crystal Structure of Wild-Type Human Phosphoglucomutase 1

All present enzymatic activity of Crystal Structure of Wild-Type Human Phosphoglucomutase 1:
5.4.2.2;

The structure of Crystal Structure of Wild-Type Human Phosphoglucomutase 1, PDB code: 5epc was solved by L.J.Beamer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	61.05 / 1.85
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	172.590, 172.590, 99.780, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 19.8

The binding sites of Magnesium atom in the Crystal Structure of Wild-Type Human Phosphoglucomutase 1 (pdb code 5epc). 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, PDB code: 5epc:
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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:9.5 occ:1.00 OD2 A:ASP288 1.9 21.8 1.0 OD1 A:ASP292 2.0 17.8 1.0 OD1 A:ASP290 2.0 20.8 1.0 OG A:SER117 2.2 26.3 1.0 O A:HOH878 2.2 26.7 1.0 O A:HOH771 2.4 30.1 1.0 CG A:ASP288 3.0 22.0 1.0 CG A:ASP290 3.0 20.2 1.0 CG A:ASP292 3.0 19.8 1.0 OD2 A:ASP290 3.3 19.2 1.0 CB A:SER117 3.4 22.0 1.0 OD1 A:ASP288 3.4 19.7 1.0 OD2 A:ASP292 3.4 24.2 1.0 CA A:SER117 4.0 22.4 1.0 CD A:ARG293 4.0 38.6 1.0 N A:ASP292 4.2 17.8 1.0 O1 A:SO4604 4.2 95.7 0.9 CB A:ASP288 4.3 17.5 1.0 CB A:ASP292 4.3 19.1 1.0 CB A:ASP290 4.4 17.3 1.0 N A:ASP290 4.5 20.0 1.0 O A:HOH724 4.6 38.4 1.0 CG A:ARG293 4.6 29.2 1.0 C A:SER117 4.6 25.7 1.0 N A:ARG293 4.6 16.7 1.0 CA A:ASP292 4.6 20.7 1.0 ND1 A:HIS118 4.7 34.9 1.0 N A:HIS118 4.7 25.4 1.0 N A:GLY291 4.7 20.2 1.0 C A:ASP292 4.8 21.1 1.0 CA A:ASP290 4.8 20.3 1.0 C A:ASP290 4.9 19.5 1.0 CB A:ARG293 4.9 21.7 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Wild-Type Human Phosphoglucomutase 1


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:24.6 occ:1.00 OD2 B:ASP288 1.9 31.7 1.0 OD1 B:ASP292 2.0 34.8 1.0 OD1 B:ASP290 2.1 30.9 1.0 O B:HOH851 2.2 36.8 1.0 OG B:SER117 2.3 36.5 1.0 CG B:ASP292 3.0 31.9 1.0 CG B:ASP290 3.0 39.5 1.0 CG B:ASP288 3.1 37.7 1.0 OD2 B:ASP290 3.3 32.0 1.0 CB B:SER117 3.3 38.5 1.0 OD2 B:ASP292 3.3 32.4 1.0 OD1 B:ASP288 3.6 30.7 1.0 CA B:SER117 3.9 42.8 1.0 O B:HOH706 4.0 53.0 1.0 N B:ASP292 4.3 28.6 1.0 CB B:ASP288 4.3 36.9 1.0 CB B:ASP292 4.3 24.9 1.0 C B:SER117 4.4 48.9 1.0 CG B:ARG293 4.4 32.2 1.0 ND1 B:HIS118 4.4 48.5 1.0 CB B:ASP290 4.4 35.6 1.0 O4 B:SO4604 4.6 91.0 0.9 N B:HIS118 4.6 42.7 1.0 N B:ASP290 4.6 33.0 1.0 N B:ARG293 4.6 32.3 1.0 CA B:ASP292 4.7 28.2 1.0 C B:ASP292 4.8 35.2 1.0 CD B:ARG293 4.8 43.7 1.0 NE B:ARG293 4.8 48.2 1.0 CA B:ASP290 4.9 30.2 1.0 N B:GLY291 4.9 29.4 1.0

K.M.Stiers, B.N.Kain, A.C.Graham, L.J.Beamer. Induced Structural Disorder As A Molecular Mechanism For Enzyme Dysfunction in Phosphoglucomutase 1 Deficiency. J.Mol.Biol. V. 428 1493 2016.
ISSN: ESSN 1089-8638
PubMed: 26972339
DOI: 10.1016/J.JMB.2016.02.032