Magnesium in PDB 3p1o: Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A, PDB code: 3p1o was solved by C.Anders, Y.Higuchi, B.Schumacher, P.Thiel, N.Kato, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.05 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	84.100, 109.740, 62.020, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 23.4

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Chlorine	(Cl)	1 atom

The binding sites of Magnesium atom in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A (pdb code 3p1o). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A, PDB code: 3p1o:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A


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 Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg235 b:19.4 occ:0.50 O A:HOH338 2.4 43.6 1.0 O A:HOH339 2.6 34.9 1.0 O A:HOH269 2.6 17.3 1.0 OE2 A:GLU2 2.6 14.0 1.0 CD A:GLU2 3.5 17.2 1.0 OE1 A:GLU2 3.8 18.7 1.0 O A:HOH369 4.5 20.6 1.0 CG A:GLU2 4.7 15.7 1.0 O A:HOH313 4.7 15.8 1.0 CA A:GLU2 4.9 12.4 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A


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 Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg236 b:46.7 occ:1.00 O A:LYS77 2.4 45.1 1.0 O A:HOH362 2.6 37.8 1.0 OE1 A:GLU80 2.8 18.9 1.0 O A:HOH387 2.8 48.2 1.0 OE2 A:GLU80 3.1 20.1 1.0 O A:HOH341 3.2 26.4 1.0 CD A:GLU80 3.2 20.8 1.0 C A:LYS77 3.5 43.2 1.0 CA A:GLY78 4.1 31.4 1.0 N A:GLY78 4.2 38.2 1.0 CA A:LYS77 4.5 46.1 1.0 CG A:GLU80 4.5 13.1 1.0 CB A:LYS77 4.8 46.6 1.0 C A:GLY78 4.8 26.0 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg237 b:38.5 occ:1.00 O A:HOH426 2.1 42.4 1.0 O A:HOH372 2.2 30.2 1.0 OE2 A:GLU89 2.2 17.3 1.0 OE2 A:GLU86 2.4 17.1 0.3 OE1 A:GLU86 2.7 18.2 0.3 CD A:GLU86 2.9 16.0 0.3 CD A:GLU89 3.2 14.2 1.0 CG A:GLU89 3.9 13.3 1.0 OE1 A:GLU89 4.1 12.1 1.0 OE1 A:GLN93 4.3 17.3 1.0 O A:HOH332 4.3 29.1 1.0 NH1 A:ARG85 4.3 20.9 1.0 CG A:GLU86 4.4 14.9 0.3 NE2 A:GLN93 4.5 16.3 1.0 CB A:GLU89 4.6 14.1 1.0 CD A:GLN93 4.8 21.1 1.0 OG1 A:THR90 4.8 14.1 0.6 CG A:GLU86 4.8 14.3 0.7 CG2 A:THR90 4.9 12.6 0.4

Magnesium binding site 4 out of 4 in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilisator Fusicoccin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg238 b:24.3 occ:1.00 O A:HOH373 2.0 49.2 1.0 OE2 A:GLU188 2.3 30.8 1.0 CD A:GLU188 3.3 26.1 1.0 CG A:GLU188 3.8 18.3 1.0 OE1 A:GLU188 4.3 22.2 1.0 O A:HOH371 5.0 39.0 1.0

C.Anders, Y.Higuchi, K.Koschinsky, M.Bartel, B.Schumacher, P.Thiel, H.Nitta, R.Preisig-Muller, G.Schlichthorl, V.Renigunta, J.Ohkanda, J.Daut, N.Kato, C.Ottmann. A Semisynthetic Fusicoccane Stabilizes A Protein-Protein Interaction and Enhances the Expression of K+ Channels at the Cell Surface Chem. Biol. V. 20 583 2013.
ISSN: ISSN 1879-1301
PubMed: 23601647
DOI: 10.1016/J.CHEMBIOL.2013.03.015