Magnesium in PDB 3cyi: Crystal Structure of Human Sulfiredoxin (Srx) in Complex with Atp:MG2+

All present enzymatic activity of Crystal Structure of Human Sulfiredoxin (Srx) in Complex with Atp:MG2+:
1.8.98.2;

The structure of Crystal Structure of Human Sulfiredoxin (Srx) in Complex with Atp:MG2+, PDB code: 3cyi was solved by T.J.Jonsson, M.S.Murray, L.C.Johnson, W.T.Lowther, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.70 / 1.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	68.530, 68.530, 51.090, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / 23.1

The binding sites of Magnesium atom in the Crystal Structure of Human Sulfiredoxin (Srx) in Complex with Atp:MG2+ (pdb code 3cyi). 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 Human Sulfiredoxin (Srx) in Complex with Atp:MG2+, PDB code: 3cyi:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human Sulfiredoxin (Srx) in Complex with Atp:MG2+


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 Human Sulfiredoxin (Srx) in Complex with Atp:MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2 b:22.5 occ:1.00 O2B A:ATP1 2.1 28.7 1.0 O1A A:ATP1 2.1 36.0 1.0 O1G A:ATP1 2.2 32.5 1.0 O A:HOH181 2.2 40.1 1.0 O A:HOH190 2.3 41.9 1.0 O A:HOH191 2.3 41.1 1.0 PB A:ATP1 3.2 28.7 1.0 PG A:ATP1 3.3 33.5 1.0 PA A:ATP1 3.3 35.7 1.0 O3A A:ATP1 3.6 29.9 1.0 O3B A:ATP1 3.7 28.0 1.0 O2G A:ATP1 3.8 31.5 1.0 NH2 A:ARG101 4.0 27.5 1.0 O5' A:ATP1 4.0 37.5 1.0 N A:GLY98 4.3 24.7 1.0 O3G A:ATP1 4.6 30.3 1.0 O2A A:ATP1 4.6 36.1 1.0 O1B A:ATP1 4.6 26.2 1.0 CA A:GLY98 4.8 23.3 1.0 O A:HOH192 5.0 45.2 1.0

T.J.Jonsson, M.S.Murray, L.C.Johnson, W.T.Lowther. Reduction of Cysteine Sulfinic Acid in Peroxiredoxin By Sulfiredoxin Proceeds Directly Through A Sulfinic Phosphoryl Ester Intermediate. J.Biol.Chem. V. 283 23846 2008.
ISSN: ISSN 0021-9258
PubMed: 18579529
DOI: 10.1074/JBC.M803244200