Magnesium in PDB 8q5c: Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475)

The structure of Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475), PDB code: 8q5c was solved by M.Konstantinidou, H.Vickery, M.A.M.Pennings, J.Virta, E.J.Visser, M.C.M.Oetelaar, M.Overmans, J.Neitz, C.Ottmann, L.Brunsveld, M.R.Arkin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.60 / 2.00
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	61.77, 149.426, 76.623, 90, 90, 90
R / Rfree (%)	21.3 / 26.2

The structure of Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475) also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Magnesium atom in the Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475) (pdb code 8q5c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475), PDB code: 8q5c:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:70.1 occ:1.00 O A:HOH511 2.3 72.9 1.0 O A:HOH454 2.6 64.4 1.0 O A:HOH403 2.8 64.8 1.0 OE2 A:GLU89 2.9 53.5 1.0 CD A:GLU89 3.6 52.3 1.0 CG A:GLU89 3.7 48.5 1.0 OE1 A:GLN93 3.7 50.9 1.0 NE2 A:GLN93 4.0 50.8 1.0 OG1 A:THR90 4.1 53.1 1.0 CD A:GLN93 4.2 51.7 1.0 CB A:GLU89 4.6 47.5 1.0 OE1 A:GLU89 4.7 52.4 1.0 O A:GLU86 4.8 43.5 1.0 N A:THR90 4.8 46.7 1.0

Magnesium binding site 2 out of 4 in the Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:61.7 occ:1.00 O A:HOH477 2.0 50.4 1.0 O A:HOH485 2.6 45.9 1.0 N A:ARG3 3.7 41.0 1.0 CG A:GLU2 3.8 45.9 1.0 O A:HOH502 3.8 52.9 1.0 CB A:GLU2 3.9 44.6 1.0 CA A:GLU2 4.0 42.4 1.0 O A:HOH495 4.1 50.1 1.0 CD A:GLU2 4.3 50.6 1.0 O A:HOH509 4.3 53.9 1.0 C A:GLU2 4.4 45.2 1.0 OE2 A:GLU2 4.4 46.5 1.0 CB A:ARG3 4.4 43.8 1.0 O A:HOH435 4.5 63.9 1.0 CA A:ARG3 4.7 45.2 1.0 N A:ALA4 5.0 43.0 1.0

Magnesium binding site 3 out of 4 in the Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475) within 5.0Å range:

Magnesium binding site 4 out of 4 in the Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Ternary Structure of 14-3-3S, C-Raf Phosphopeptide (PS259) and Compound 12 (1075475) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg306 b:48.8 occ:1.00 O A:ALA203 2.0 48.0 1.0 O A:HOH440 2.1 45.0 0.5 O A:HOH433 2.7 49.4 1.0 C A:ALA203 3.2 45.0 1.0 CA A:ALA203 3.9 50.2 1.0 N A:ASP204 4.2 45.9 1.0 OD1 A:ASP204 4.3 46.3 1.0 CA A:ASP204 4.4 45.8 1.0 O A:HOH458 4.5 51.0 1.0 CB A:ALA203 4.5 48.3 1.0 CD2 A:HIS206 4.7 45.3 1.0 O A:HOH500 4.7 52.2 1.0 O A:MET202 4.7 44.5 1.0

M.Konstantinidou, H.Vickery, M.A.M.Pennings, J.Virta, E.J.Visser, M.C.M.Oetelaar, M.Overmans, J.Neitz, C.Ottmann, L.Brunsveld, M.R.Arkin. Small Molecule Stabilization of the 14-3-3SIGMA/Craf Complex Inhibits the Mapk Pathway To Be Published.