Magnesium in PDB 6y3o: 14-3-3 Sigma in Complex with Phosphorylated CAMKK2 Peptide

The structure of 14-3-3 Sigma in Complex with Phosphorylated CAMKK2 Peptide, PDB code: 6y3o was solved by A.Ballone, R.A.Lau, F.P.A.Zweipfenning, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.53 / 1.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.509, 112.497, 62.433, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 19.8

The structure of 14-3-3 Sigma in Complex with Phosphorylated CAMKK2 Peptide also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Magnesium atom in the 14-3-3 Sigma in Complex with Phosphorylated CAMKK2 Peptide (pdb code 6y3o). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the 14-3-3 Sigma in Complex with Phosphorylated CAMKK2 Peptide, PDB code: 6y3o:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the 14-3-3 Sigma in Complex with Phosphorylated CAMKK2 Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 14-3-3 Sigma in Complex with Phosphorylated CAMKK2 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:22.5 occ:0.00 O A:HOH605 2.2 28.1 1.0 O A:ALA-3 2.3 31.9 1.0 OG A:SER0 2.4 22.5 1.0 N A:SER0 2.9 17.3 1.0 C A:ALA-3 3.1 27.9 1.0 CB A:SER0 3.3 19.1 1.0 N A:GLY-1 3.3 19.1 1.0 C A:MET-2 3.3 18.0 1.0 CA A:MET-2 3.4 22.2 1.0 CA A:SER0 3.5 16.9 1.0 N A:MET-2 3.6 25.8 1.0 O A:MET-2 3.9 17.1 1.0 C A:GLY-1 3.9 17.2 1.0 N A:MET1 4.0 13.3 1.0 C A:SER0 4.1 15.2 1.0 CA A:GLY-1 4.1 17.4 1.0 CA A:ALA-3 4.2 30.7 1.0 O A:GLY-4 4.4 31.4 1.0 O A:HOH617 4.4 29.7 1.0 CB A:MET-2 4.9 19.2 1.0

Magnesium binding site 2 out of 2 in the 14-3-3 Sigma in Complex with Phosphorylated CAMKK2 Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of 14-3-3 Sigma in Complex with Phosphorylated CAMKK2 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:13.4 occ:1.00 O A:GLU110 2.3 20.3 1.0 O A:HOH509 2.4 27.2 1.0 OE2 A:GLU35 2.4 23.2 1.0 O A:HOH661 2.4 24.4 1.0 OE1 A:GLU35 2.8 25.3 1.0 CD A:GLU35 2.9 24.1 1.0 C A:GLU110 3.5 20.5 1.0 O A:HOH680 4.1 30.5 1.0 N A:GLY112 4.1 18.3 1.0 CA A:GLU110 4.3 17.6 1.0 CG A:GLU35 4.4 20.7 1.0 N A:ALA111 4.5 17.0 1.0 CB A:GLU110 4.5 22.8 1.0 CA A:ALA111 4.6 16.6 1.0 O A:HOH543 4.6 25.9 1.0 OE1 A:GLU110 4.6 28.2 1.0 C A:ALA111 4.7 19.1 1.0 CA A:GLY112 4.9 20.0 1.0 O A:HOH523 4.9 23.6 1.0 O A:HOH620 5.0 35.4 1.0

A.Ballone, R.A.Lau, F.P.A.Zweipfenning, C.Ottmann. A New Soaking Procedure For X-Ray Crystallographic Structural Determination of Protein-Peptide Complexes. Acta Crystallogr.,Sect.F V. 76 501 2020.
ISSN: ESSN 2053-230X
PubMed: 33006579
DOI: 10.1107/S2053230X2001122X