Magnesium in PDB 3sp5: Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenol

The structure of Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenol, PDB code: 3sp5 was solved by C.Anders, B.Schumacher, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.49 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	81.800, 111.560, 62.400, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 21.1

The binding sites of Magnesium atom in the Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenol (pdb code 3sp5). 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 C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenol, PDB code: 3sp5:
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 C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenol


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 C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg233 b:11.1 occ:1.00 O A:HOH255 2.3 16.6 1.0 O A:HOH458 2.3 26.6 1.0 O A:HOH305 2.3 21.1 1.0 O A:GLU110 2.3 12.4 1.0 OE2 A:GLU35 2.5 16.8 1.0 OE1 A:GLU35 2.6 19.4 1.0 CD A:GLU35 2.9 18.4 1.0 C A:GLU110 3.6 12.8 1.0 N A:GLY112 3.9 16.2 1.0 CG A:GLU35 4.4 13.8 1.0 CA A:GLU110 4.5 12.2 1.0 CA A:ALA111 4.5 12.2 1.0 N A:ALA111 4.5 10.7 1.0 CA A:GLY112 4.6 15.3 1.0 C A:ALA111 4.6 14.5 1.0 OE1 A:GLU110 4.7 28.6 1.0 CB A:GLU110 4.7 14.2 1.0 O A:HOH338 4.9 20.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenol


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 C38V/N166H in Complex with Task-3 Peptide and Stabilizer Cotylenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg234 b:16.9 occ:1.00 O A:HOH308 2.1 36.5 1.0 OE1 A:GLU75 2.2 27.5 1.0 O A:HOH313 2.3 27.4 1.0 O A:HOH306 2.5 49.6 1.0 O A:HOH263 3.1 39.5 1.0 CD A:GLU75 3.3 29.3 1.0 CG A:GLU75 3.7 34.5 1.0 OE2 A:GLU75 4.4 31.6 1.0 O A:GLY73 4.6 41.3 0.8 CB A:GLU75 4.9 36.6 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 1074-5521
PubMed: 23601647
DOI: 10.1016/J.CHEMBIOL.2013.03.015