Magnesium in PDB 3p1s: 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: 3p1s 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)	19.83 / 1.65
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.210, 111.180, 62.350, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / 20.1

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:

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 3p1s). 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: 3p1s:
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:16.8 occ:1.00 O A:GLU161 2.3 17.6 1.0 O A:HOH273 2.5 26.6 1.0 O A:HOH360 2.5 22.6 1.0 C A:GLU161 3.4 12.8 1.0 CA A:MET162 4.3 11.2 0.4 N A:MET162 4.3 11.8 1.0 CA A:GLU161 4.3 13.4 1.0 CA A:MET162 4.3 11.2 0.6 OE2 A:GLU115 4.4 30.8 1.0 CB A:GLU161 4.8 13.5 1.0 CD A:PRO163 4.8 12.1 1.0 OE1 A:GLU161 4.8 32.0 1.0 O A:HOH478 4.9 30.6 1.0 CG A:MET162 4.9 10.6 0.4

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:10.7 occ:0.50 O A:HOH355 2.3 30.5 1.0 OE1 A:GLU2 2.4 13.1 1.0 O A:HOH280 2.5 13.0 1.0 CD A:GLU2 3.4 12.7 1.0 OE2 A:GLU2 3.7 14.4 1.0 O A:HOH320 4.3 12.8 1.0 O A:HOH281 4.5 12.4 1.0 CG A:GLU2 4.7 10.9 1.0 CA A:GLU2 4.8 8.4 1.0 N A:ARG3 4.9 7.3 1.0 O A:HOH300 4.9 19.6 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