Magnesium in PDB 5mxm: The X-Ray Structure of Human M190I Phosphoglycerate Kinase 1 Mutant

All present enzymatic activity of The X-Ray Structure of Human M190I Phosphoglycerate Kinase 1 Mutant:
2.7.2.3;

The structure of The X-Ray Structure of Human M190I Phosphoglycerate Kinase 1 Mutant, PDB code: 5mxm was solved by A.Ilari, A.Fiorillo, A.Cipollone, M.Petrosino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	69.91 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.363, 91.104, 109.010, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 22.6

The binding sites of Magnesium atom in the The X-Ray Structure of Human M190I Phosphoglycerate Kinase 1 Mutant (pdb code 5mxm). 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 The X-Ray Structure of Human M190I Phosphoglycerate Kinase 1 Mutant, PDB code: 5mxm:

Magnesium binding site 1 out of 1 in the The X-Ray Structure of Human M190I Phosphoglycerate Kinase 1 Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The X-Ray Structure of Human M190I Phosphoglycerate Kinase 1 Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:19.7 occ:1.00 O2A A:ADP503 2.0 18.5 1.0 O3B A:ADP503 2.0 18.2 1.0 O A:HOH722 2.1 21.1 1.0 O A:HOH759 2.1 18.8 1.0 OD2 A:ASP374 2.1 17.6 1.0 O A:HOH732 2.2 17.9 1.0 PB A:ADP503 3.3 19.7 1.0 PA A:ADP503 3.3 21.5 1.0 CG A:ASP374 3.3 14.3 1.0 O3A A:ADP503 3.5 19.5 1.0 O2B A:ADP503 3.8 17.2 1.0 CB A:ASP374 4.0 14.3 1.0 O A:HOH754 4.0 33.8 1.0 N A:ASP374 4.0 14.9 1.0 O A:HOH851 4.1 32.2 1.0 O A:HOH799 4.1 30.8 1.0 O2 A:3PG502 4.2 16.5 1.0 NZ A:LYS215 4.2 27.6 1.0 OD1 A:ASP374 4.2 12.4 1.0 O A:HOH726 4.2 13.5 1.0 O5' A:ADP503 4.3 22.1 1.0 C5' A:ADP503 4.3 20.3 1.0 O A:HOH756 4.4 20.3 1.0 O1A A:ADP503 4.5 21.2 1.0 CE A:LYS215 4.5 27.4 1.0 O1B A:ADP503 4.5 14.3 1.0 O A:HOH717 4.6 25.4 1.0 O A:HOH636 4.6 32.8 1.0 CA A:ASP374 4.7 14.3 1.0 CD A:LYS215 4.7 28.2 1.0 O1 A:3PG502 4.7 19.2 1.0 N A:GLY373 4.7 14.7 1.0 C1 A:3PG502 4.9 16.1 1.0 CA A:GLY373 4.9 15.0 1.0 C A:GLY373 5.0 15.3 1.0

A.Fiorillo, M.Petrosino, A.Ilari, A.Pasquo, A.Cipollone, M.Maggi, R.Chiaraluce, V.Consalvi. The Phosphoglycerate Kinase 1 Variants Found in Carcinoma Cells Display Different Catalytic Activity and Conformational Stability Compared to the Native Enzyme. Plos One V. 13 99191 2018.
ISSN: ESSN 1932-6203
PubMed: 29995887
DOI: 10.1371/JOURNAL.PONE.0199191