Magnesium in PDB 5zyd: Crystal Structure of Glucose Isomerase Soaked with Glucose

All present enzymatic activity of Crystal Structure of Glucose Isomerase Soaked with Glucose:
5.3.1.5;

The structure of Crystal Structure of Glucose Isomerase Soaked with Glucose, PDB code: 5zyd was solved by K.H.Nam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.70 / 1.40
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	92.505, 97.820, 102.297, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 16.5

The binding sites of Magnesium atom in the Crystal Structure of Glucose Isomerase Soaked with Glucose (pdb code 5zyd). 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 Crystal Structure of Glucose Isomerase Soaked with Glucose, PDB code: 5zyd:

Magnesium binding site 1 out of 1 in the Crystal Structure of Glucose Isomerase Soaked with Glucose


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 Glucose Isomerase Soaked with Glucose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:14.1 occ:1.00 OE2 A:GLU217 1.9 13.9 1.0 OD2 A:ASP287 2.0 17.4 1.0 OE2 A:GLU181 2.1 15.1 1.0 O A:HOH520 2.1 16.0 1.0 OD2 A:ASP245 2.1 14.0 1.0 O A:HOH638 2.2 16.6 1.0 CD A:GLU181 3.0 13.8 1.0 CD A:GLU217 3.0 12.1 1.0 OE1 A:GLU181 3.2 11.9 1.0 CG A:ASP287 3.2 11.2 1.0 CG A:ASP245 3.3 12.0 1.0 CB A:ASP287 3.7 8.9 1.0 OE1 A:GLU217 3.7 13.8 1.0 O A:HOH811 3.8 17.3 1.0 CB A:ASP245 3.9 8.9 1.0 O A:HOH667 4.0 22.1 1.0 OD1 A:ASP287 4.2 10.5 1.0 CG A:GLU217 4.2 9.0 1.0 CE1 A:HIS220 4.2 8.7 1.0 OD1 A:ASP245 4.2 12.2 1.0 CG A:GLU181 4.3 9.2 1.0 CB A:GLU217 4.4 7.4 1.0 NE2 A:HIS220 4.6 9.0 1.0 ND2 A:ASN215 4.7 9.6 1.0 O A:HOH838 4.9 20.5 1.0

J.E.Bae, K.Y.Hwang, K.H.Nam. Structural Analysis of Substrate Recognition By Glucose Isomerase in MN2+Binding Mode at M2 Site in S. Rubiginosus Biochem. Biophys. Res. V. 503 770 2018COMMUN..
ISSN: ESSN 1090-2104
PubMed: 29909012
DOI: 10.1016/J.BBRC.2018.06.074