Magnesium in PDB 2gpc: The Crystal Structure of the Enzyme Fe-Superoxide Dismutase From Trypanosoma Cruzi

The structure of The Crystal Structure of the Enzyme Fe-Superoxide Dismutase From Trypanosoma Cruzi, PDB code: 2gpc was solved by M.V.A.S.Navarro, R.C.Garratt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.49 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	109.626, 38.985, 91.073, 90.00, 105.85, 90.00
R / Rfree (%)	15.4 / 19.8

The structure of The Crystal Structure of the Enzyme Fe-Superoxide Dismutase From Trypanosoma Cruzi also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Magnesium atom in the The Crystal Structure of the Enzyme Fe-Superoxide Dismutase From Trypanosoma Cruzi (pdb code 2gpc). 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 Crystal Structure of the Enzyme Fe-Superoxide Dismutase From Trypanosoma Cruzi, PDB code: 2gpc:

Magnesium binding site 1 out of 1 in the The Crystal Structure of the Enzyme Fe-Superoxide Dismutase From Trypanosoma Cruzi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of the Enzyme Fe-Superoxide Dismutase From Trypanosoma Cruzi within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg496 b:42.6 occ:1.00 O A:HOH501 2.1 23.8 1.0 O A:HOH500 2.1 25.8 1.0 O A:HOH498 2.2 40.0 1.0 O A:HOH497 2.2 30.3 1.0 O A:HOH499 2.3 20.0 1.0 O A:HOH737 3.7 37.1 1.0 OE2 A:GLU80 4.0 17.0 1.0 OE1 A:GLU80 4.1 15.1 1.0 O A:HOH539 4.2 16.9 1.0 CD A:GLU80 4.5 14.2 1.0 O A:HOH655 4.5 25.4 1.0 CG2 A:THR76 4.7 10.2 1.0

J.F.Bachega, M.V.Navarro, L.Bleicher, R.K.Bortoleto-Bugs, D.Dive, P.Hoffmann, E.Viscogliosi, R.C.Garratt. Systematic Structural Studies of Iron Superoxide Dismutases From Human Parasites and A Statistical Coupling Analysis of Metal Binding Specificity Proteins V. 77 26 2009.
ISSN: ISSN 0887-3585
PubMed: 19384994
DOI: 10.1002/PROT.22412