Magnesium in PDB 4dat: Structure of 14-3-3 Sigma in Complex with PADI6 14-3-3 Binding Motif II

All present enzymatic activity of Structure of 14-3-3 Sigma in Complex with PADI6 14-3-3 Binding Motif II:
3.5.3.15;

The structure of Structure of 14-3-3 Sigma in Complex with PADI6 14-3-3 Binding Motif II, PDB code: 4dat was solved by R.Rose, M.Rose, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.58 / 1.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.220, 112.360, 62.730, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 18.3

The binding sites of Magnesium atom in the Structure of 14-3-3 Sigma in Complex with PADI6 14-3-3 Binding Motif II (pdb code 4dat). 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 Structure of 14-3-3 Sigma in Complex with PADI6 14-3-3 Binding Motif II, PDB code: 4dat:

Magnesium binding site 1 out of 1 in the Structure of 14-3-3 Sigma in Complex with PADI6 14-3-3 Binding Motif II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of 14-3-3 Sigma in Complex with PADI6 14-3-3 Binding Motif II within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:16.4 occ:1.00 OE2 A:GLU35 2.1 18.7 1.0 O A:GLU110 2.3 18.7 0.5 O A:GLU110 2.3 18.4 0.5 O A:HOH533 2.4 27.4 1.0 O A:HOH522 2.4 27.6 1.0 O A:HOH530 2.4 25.1 1.0 OE1 A:GLU35 2.6 29.0 1.0 CD A:GLU35 2.7 23.7 1.0 C A:GLU110 3.5 16.5 0.5 C A:GLU110 3.5 16.6 0.5 N A:GLY112 4.0 19.0 1.0 CG A:GLU35 4.2 18.3 1.0 CA A:GLU110 4.3 15.5 0.5 CA A:GLU110 4.4 15.4 0.5 N A:ALA111 4.4 15.7 1.0 CA A:ALA111 4.5 16.3 1.0 O A:HOH542 4.6 32.4 1.0 CB A:GLU110 4.6 16.8 0.5 CB A:GLU110 4.6 16.4 0.5 C A:ALA111 4.7 16.9 1.0 OE1 A:GLU110 4.7 25.3 0.5 CA A:GLY112 4.8 20.9 1.0 O A:HOH454 4.9 27.5 1.0

R.Rose, M.Rose, C.Ottmann. Identification and Structural Characterization of Two 14-3-3 Binding Sites in the Human Peptidylarginine Deiminase Type VI. J.Struct.Biol. V. 180 65 2012.
ISSN: ISSN 1047-8477
PubMed: 22634725
DOI: 10.1016/J.JSB.2012.05.010