Magnesium in PDB 3p1q: Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A

The structure of Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A, PDB code: 3p1q 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)	19.57 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.460, 110.700, 62.200, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 21.7

The structure of Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer 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 C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A (pdb code 3p1q). 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 Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A, PDB code: 3p1q:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer 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 C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg251 b:11.0 occ:1.00 O A:GLU110 2.2 17.8 1.0 O A:HOH397 2.3 24.0 1.0 O A:HOH423 2.4 25.8 1.0 OE1 A:GLU35 2.4 22.7 1.0 OE2 A:GLU35 2.7 24.7 1.0 CD A:GLU35 2.9 20.0 1.0 C A:GLU110 3.5 15.5 1.0 N A:GLY112 4.2 15.9 1.0 CG A:GLU35 4.3 14.5 1.0 CA A:GLU110 4.4 15.7 0.5 CA A:GLU110 4.4 15.8 0.5 N A:ALA111 4.4 13.3 1.0 CB A:GLU110 4.5 16.6 0.5 CA A:ALA111 4.6 14.4 1.0 CB A:GLU110 4.6 16.1 0.5 OE1 A:GLU110 4.7 15.8 0.5 C A:ALA111 4.8 16.2 1.0 CA A:GLY112 4.8 16.6 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide and Stabilizer 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 C38N/N166H in Complex with Task-3 Peptide and Stabilizer Fusicoccin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg252 b:9.5 occ:0.50 OE1 A:GLU2 2.4 14.1 1.0 O A:HOH334 2.4 31.4 1.0 O A:HOH262 2.5 13.2 1.0 CD A:GLU2 3.4 13.1 1.0 OE2 A:GLU2 3.7 12.9 1.0 O A:HOH287 4.3 14.2 1.0 O A:HOH291 4.5 15.2 1.0 CG A:GLU2 4.7 10.3 1.0 CA A:GLU2 4.8 9.3 1.0 N A:ARG3 4.9 8.0 1.0 CB A:GLU2 5.0 9.3 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