Magnesium in PDB 7obk: Crystal Structure of 14-3-3 Sigma in Complex with Pkr Phosphopeptide

All present enzymatic activity of Crystal Structure of 14-3-3 Sigma in Complex with Pkr Phosphopeptide:
2.7.10.2; 2.7.11.1;

The structure of Crystal Structure of 14-3-3 Sigma in Complex with Pkr Phosphopeptide, PDB code: 7obk was solved by F.Centorrino, B.Andlovic, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.86 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.714, 112.56, 62.623, 90, 90, 90
R / Rfree (%)	14.5 / 18.3

The binding sites of Magnesium atom in the Crystal Structure of 14-3-3 Sigma in Complex with Pkr Phosphopeptide (pdb code 7obk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of 14-3-3 Sigma in Complex with Pkr Phosphopeptide, PDB code: 7obk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of 14-3-3 Sigma in Complex with Pkr Phosphopeptide


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 14-3-3 Sigma in Complex with Pkr Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:2.3 occ:0.50 O A:HOH657 2.4 33.6 1.0 OE1 A:GLU2 2.4 10.7 1.0 O A:HOH498 2.6 7.3 1.0 CD A:GLU2 3.4 9.7 1.0 OE2 A:GLU2 3.9 8.6 1.0 HA A:GLU2 4.0 5.6 1.0 H A:ARG3 4.2 4.9 1.0 O A:HOH609 4.3 5.9 1.0 O A:HOH795 4.5 7.0 1.0 HB3 A:GLU2 4.6 7.9 1.0 CG A:GLU2 4.7 3.2 1.0 CA A:GLU2 4.8 4.6 1.0 CB A:GLU2 4.9 6.6 1.0 HG2 A:GLU2 4.9 3.9 1.0 N A:ARG3 5.0 4.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of 14-3-3 Sigma in Complex with Pkr Phosphopeptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of 14-3-3 Sigma in Complex with Pkr Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:0.9 occ:1.00 O A:GLU110 2.3 8.1 0.5 O A:GLU110 2.3 8.1 0.5 O A:HOH642 2.3 17.2 1.0 O A:HOH672 2.4 12.8 1.0 OE2 A:GLU35 2.4 11.8 1.0 OE1 A:GLU35 2.6 14.8 1.0 CD A:GLU35 2.8 17.9 1.0 H A:GLY112 3.5 10.8 1.0 C A:GLU110 3.5 10.2 0.5 C A:GLU110 3.5 10.2 0.5 HB3 A:GLU110 3.7 12.9 0.5 HA A:ALA111 3.8 7.1 1.0 HB3 A:GLU110 3.9 13.7 0.5 N A:GLY112 4.1 9.0 1.0 HA A:GLU110 4.3 9.1 0.5 HA A:GLU110 4.3 9.4 0.5 CG A:GLU35 4.4 10.7 1.0 CA A:GLU110 4.4 7.8 0.5 O A:HOH712 4.4 31.9 1.0 CA A:GLU110 4.4 7.6 0.5 N A:ALA111 4.4 6.2 1.0 HA3 A:GLY112 4.4 12.7 1.0 CB A:GLU110 4.5 10.8 0.5 CA A:ALA111 4.5 5.9 1.0 O A:HOH567 4.6 15.7 1.0 O A:HOH425 4.6 25.6 1.0 HG2 A:GLU35 4.6 12.9 1.0 CB A:GLU110 4.6 11.4 0.5 C A:ALA111 4.7 9.7 1.0 HG3 A:GLU35 4.7 12.9 1.0 OE1 A:GLU110 4.8 6.9 0.5 O A:HOH574 4.8 12.2 1.0 O A:HOH689 4.9 27.7 1.0 CA A:GLY112 4.9 10.6 1.0 HB2 A:GLU110 4.9 12.9 0.5

B.Andlovic, G.Heilmann, S.Ninck, S.Andrei, F.Centorrino, Y.Higuchi, N.Kato, L.Brunsveld, S.Menninger, A.Choidas, A.Wolf, M.Kaiser, J.Eickhoff, C.Ottmann. Inf Alpha Primes Ovarian Cancer Cells For Fusicoccin-Induced Cell Death Via Stabilization of 14-3-3 Protein-Protein Interactions To Be Published.