Magnesium in PDB 6y8a: 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} Peptide

All present enzymatic activity of 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} Peptide:
2.7.11.17;

The structure of 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} Peptide, PDB code: 6y8a 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)	29.33 / 1.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.243, 112.139, 62.821, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 20.1

The structure of 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} Peptide also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} Peptide (pdb code 6y8a). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} Peptide, PDB code: 6y8a:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} 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{PS511} Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:26.1 occ:0.00 OE2 A:GLU188 1.7 21.9 1.0 CD A:GLU188 2.2 18.5 1.0 CG A:GLU188 2.8 18.0 1.0 OE1 A:GLU188 3.1 24.5 1.0 O A:HOH483 3.4 27.8 1.0 CB A:GLU188 3.7 15.6 1.0 O A:HOH562 4.4 27.3 1.0 O A:HOH739 4.7 36.5 1.0 CA A:GLU188 4.8 14.1 1.0

Magnesium binding site 2 out of 3 in the 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} 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{PS511} Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:24.4 occ:0.00 O A:HOH685 2.3 36.7 1.0 O A:HOH457 2.3 30.5 1.0 OE2 A:GLU89 2.5 20.2 1.0 CD A:GLU89 3.5 16.2 1.0 O A:HOH489 4.0 31.3 1.0 O A:HOH581 4.2 34.5 1.0 CG A:GLU89 4.3 15.9 1.0 NH1 A:ARG85 4.3 20.6 1.0 OE1 A:GLU89 4.3 16.0 1.0 CG A:GLU86 4.7 20.8 1.0 OE1 A:GLN93 4.7 19.5 1.0 O A:HOH418 4.8 40.3 1.0 NE2 A:GLN93 4.9 19.0 1.0 CB A:GLU89 4.9 15.1 1.0

Magnesium binding site 3 out of 3 in the 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of 14-3-3 Sigma in Complex with Phosphorylated CAMKK2{PS511} Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:22.6 occ:0.00 O A:HOH634 2.2 32.5 1.0 OE1 A:GLU2 2.4 18.4 1.0 O A:HOH440 2.5 18.1 1.0 O A:HOH675 2.6 34.4 1.0 CD A:GLU2 3.4 19.8 1.0 OE2 A:GLU2 3.7 17.0 1.0 O A:HOH599 4.2 17.5 1.0 O A:HOH754 4.5 19.7 1.0 CG A:GLU2 4.7 15.3 1.0 CA A:GLU2 4.9 12.4 1.0 N A:ARG3 4.9 13.4 1.0 CB A:GLU2 5.0 12.4 1.0 O A:HOH491 5.0 24.5 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