Magnesium in PDB 5f9c: Crystal Structure of the G121R Mutant of Human Phosphoglucomutase 1

All present enzymatic activity of Crystal Structure of the G121R Mutant of Human Phosphoglucomutase 1:
5.4.2.2;

The structure of Crystal Structure of the G121R Mutant of Human Phosphoglucomutase 1, PDB code: 5f9c 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)	60.94 / 2.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	171.980, 171.980, 99.900, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 24.3

The binding sites of Magnesium atom in the Crystal Structure of the G121R Mutant of Human Phosphoglucomutase 1 (pdb code 5f9c). 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 the G121R Mutant of Human Phosphoglucomutase 1, PDB code: 5f9c:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the G121R Mutant of 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 the G121R Mutant of Human Phosphoglucomutase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:67.6 occ:1.00 OD2 A:ASP288 1.9 69.4 1.0 OD1 A:ASP292 2.0 66.2 1.0 OD1 A:ASP290 2.3 59.7 1.0 OG A:SER117 2.8 0.4 1.0 CG A:ASP292 2.9 69.7 1.0 CG A:ASP288 3.1 67.0 1.0 OD2 A:ASP292 3.3 74.6 1.0 CG A:ASP290 3.3 60.1 1.0 OD2 A:ASP290 3.7 55.8 1.0 OD1 A:ASP288 3.7 65.2 1.0 NE A:ARG293 3.9 80.9 1.0 CB A:SER117 4.0 0.7 1.0 CA A:SER117 4.1 93.7 1.0 CB A:ASP292 4.2 63.3 1.0 CG A:ARG293 4.3 49.8 1.0 CD A:ARG293 4.3 61.2 1.0 CB A:ASP288 4.3 60.9 1.0 N A:ASP292 4.3 47.9 1.0 N A:ASP290 4.4 70.2 1.0 CB A:ASP290 4.6 60.1 1.0 N A:ARG293 4.6 39.0 1.0 CA A:ASP292 4.6 51.4 1.0 C A:SER117 4.7 99.0 1.0 CZ A:ARG293 4.7 95.2 1.0 C A:ASP292 4.8 46.1 1.0 CB A:ARG293 4.9 43.3 1.0 N A:GLY291 4.9 59.0 1.0 CA A:ASP290 4.9 63.4 1.0 N A:GLY289 5.0 82.6 1.0 NH2 A:ARG293 5.0 0.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the G121R Mutant of 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 the G121R Mutant of Human Phosphoglucomutase 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg607 b:0.8 occ:1.00 OD2 B:ASP288 2.7 84.5 1.0 OD1 B:ASP292 2.9 0.5 1.0 NH1 B:ARG293 2.9 0.6 1.0 OD1 B:ASP290 3.4 98.6 1.0 CG B:ASP292 3.8 0.4 1.0 OD2 B:ASP292 3.8 99.1 1.0 CZ B:ARG293 4.0 0.7 1.0 CG B:ASP288 4.0 85.6 1.0 CD B:ARG293 4.0 95.8 1.0 CG B:ASP290 4.2 96.8 1.0 OD2 B:ASP290 4.3 97.8 1.0 NE B:ARG293 4.3 0.1 1.0 CG B:ARG293 4.4 78.4 1.0 OD1 B:ASP288 4.8 84.5 1.0 CB B:ASP288 4.9 83.7 1.0 NH2 B:ARG293 5.0 0.1 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