Magnesium in PDB 4mif: Pyranose 2-Oxidase From Phanerochaete Chrysosporium, Wild Type From Natural Source

All present enzymatic activity of Pyranose 2-Oxidase From Phanerochaete Chrysosporium, Wild Type From Natural Source:
1.1.3.10;

The structure of Pyranose 2-Oxidase From Phanerochaete Chrysosporium, Wild Type From Natural Source, PDB code: 4mif was solved by N.Hassan, T.C.Tan, O.Spadiut, I.Pisanelli, L.Fusco, D.Haltrich, C.Peterbauer, C.Divne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.40 / 1.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	164.034, 164.034, 232.521, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 17.1

The binding sites of Magnesium atom in the Pyranose 2-Oxidase From Phanerochaete Chrysosporium, Wild Type From Natural Source (pdb code 4mif). 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 Pyranose 2-Oxidase From Phanerochaete Chrysosporium, Wild Type From Natural Source, PDB code: 4mif:

Magnesium binding site 1 out of 1 in the Pyranose 2-Oxidase From Phanerochaete Chrysosporium, Wild Type From Natural Source


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Pyranose 2-Oxidase From Phanerochaete Chrysosporium, Wild Type From Natural Source within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg802 b:29.7 occ:1.00 O B:HOH903 2.1 25.4 1.0 OE1 B:GLU202 2.2 31.3 1.0 O B:HOH904 2.2 25.0 1.0 O B:HOH901 2.2 24.9 1.0 O B:HOH902 2.2 24.4 1.0 CD B:GLU202 3.3 42.5 1.0 CG B:GLU202 4.0 36.9 1.0 O B:HOH1244 4.2 37.6 1.0 OE2 B:GLU202 4.3 44.1 1.0 CA B:GLU202 4.4 22.9 1.0 O B:GLU202 4.5 23.5 1.0 CB B:GLU202 4.7 29.2 1.0 NH2 B:ARG260 4.9 28.5 1.0 C B:GLU202 5.0 21.8 1.0

N.Hassan, T.C.Tan, O.Spadiut, I.Pisanelli, L.Fusco, D.Haltrich, C.K.Peterbauer, C.Divne. Crystal Structures of Phanerochaete Chrysosporium Pyranose 2-Oxidase Suggest That the N-Terminus Acts As A Propeptide That Assists in Homotetramer Assembly. Febs Open Bio V. 3 496 2013.
ISSN: ESSN 2211-5463
PubMed: 24282677
DOI: 10.1016/J.FOB.2013.10.010