Magnesium in PDB 5o84: Glutathione S-Transferase Tau 23 (Partially Oxidized)

All present enzymatic activity of Glutathione S-Transferase Tau 23 (Partially Oxidized):
2.5.1.18;

The structure of Glutathione S-Transferase Tau 23 (Partially Oxidized), PDB code: 5o84 was solved by D.R.Young, I.Van Molle, M.Tossounian, J.Messens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.26 / 1.88
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	85.165, 50.740, 57.167, 90.00, 112.47, 90.00
R / Rfree (%)	18.1 / 21.6

The binding sites of Magnesium atom in the Glutathione S-Transferase Tau 23 (Partially Oxidized) (pdb code 5o84). 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 Glutathione S-Transferase Tau 23 (Partially Oxidized), PDB code: 5o84:

Magnesium binding site 1 out of 1 in the Glutathione S-Transferase Tau 23 (Partially Oxidized)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Glutathione S-Transferase Tau 23 (Partially Oxidized) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:29.5 occ:1.00 O A:HOH444 2.0 24.0 1.0 O A:HOH467 2.0 32.1 0.9 O A:HOH513 2.0 28.7 0.8 O A:HOH429 2.1 26.9 0.9 O A:HOH475 2.1 31.6 1.0 O A:HOH517 2.1 27.5 0.6 O A:ILE84 4.0 24.6 1.0 O A:HOH499 4.2 32.5 1.0 O A:PHE150 4.4 19.7 1.0 O A:HOH511 4.4 37.2 1.0 O A:PRO83 4.4 24.4 1.0 CA A:PRO86 4.5 29.5 1.0 CB A:GLU149 4.5 27.7 1.0 O A:LEU85 4.5 23.2 1.0 N A:PRO86 4.5 25.9 1.0 C A:LEU85 4.6 22.9 1.0 C A:ILE84 4.8 25.9 1.0 O A:GLU149 4.8 23.7 1.0 O A:GLY146 4.8 30.4 1.0 CA A:GLY151 4.9 18.2 1.0

M.A.Tossounian, I.Van Molle, K.Wahni, S.Jacques, K.Gevaert, F.Van Breusegem, D.Vertommen, D.Young, L.A.Rosado, J.Messens. Disulfide Bond Formation Protects Arabidopsis Thaliana Glutathione Transferase Tau 23 From Oxidative Damage. Biochim. Biophys. Acta V.1862 775 2018.
ISSN: ISSN 0006-3002
PubMed: 29031766
DOI: 10.1016/J.BBAGEN.2017.10.007