Magnesium in PDB 4fr3: Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer 16-O-Me-Fc-H

The structure of Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer 16-O-Me-Fc-H, PDB code: 4fr3 was solved by C.Ottmann, C.Anders, B.Schumacher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.65 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	81.680, 111.990, 62.970, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 20.9

The binding sites of Magnesium atom in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer 16-O-Me-Fc-H (pdb code 4fr3). 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 in Complex with Task-3 Peptide and Stabilizer 16-O-Me-Fc-H, PDB code: 4fr3:
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 in Complex with Task-3 Peptide and Stabilizer 16-O-Me-Fc-H


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 Stabilizer 16-O-Me-Fc-H within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:16.0 occ:1.00 O A:HOH401 2.2 25.2 1.0 OE2 A:GLU35 2.2 30.1 1.0 O A:HOH520 2.2 26.7 1.0 O A:GLU110 2.2 18.4 1.0 OE1 A:GLU35 2.2 30.6 1.0 O A:HOH521 2.5 27.7 1.0 CD A:GLU35 2.6 30.9 1.0 C A:GLU110 3.5 18.8 1.0 N A:GLY112 4.0 21.3 1.0 CG A:GLU35 4.1 23.3 1.0 CA A:GLU110 4.4 19.1 1.0 N A:ALA111 4.4 16.9 1.0 CB A:GLU110 4.5 20.4 1.0 CA A:ALA111 4.5 18.2 1.0 O A:HOH421 4.6 31.0 1.0 OE1 A:GLU110 4.6 35.5 1.0 C A:ALA111 4.7 20.0 1.0 O A:HOH503 4.7 31.3 1.0 CA A:GLY112 4.7 22.6 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human 14-3-3 Sigma in Complex with Task-3 Peptide and Stabilizer 16-O-Me-Fc-H


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 Stabilizer 16-O-Me-Fc-H within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:15.1 occ:0.50 O A:HOH523 2.2 25.1 1.0 O A:HOH402 2.2 21.3 0.5 OE1 A:GLU2 2.2 22.4 1.0 O A:HOH425 2.2 17.4 1.0 CD A:GLU2 3.3 21.8 1.0 OE2 A:GLU2 3.8 22.7 1.0 O A:HOH419 4.1 17.1 1.0 O A:HOH432 4.4 19.2 1.0 CG A:GLU2 4.6 15.6 1.0 CA A:GLU2 4.7 14.5 1.0 N A:ARG3 4.7 12.6 1.0 CB A:GLU2 4.8 13.8 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