Magnesium in PDB 3p1p: Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide

The structure of Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide, PDB code: 3p1p 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)	19.80 / 1.95
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	80.210, 109.410, 61.220, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 22.7

The structure of Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide 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 (pdb code 3p1p). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide, PDB code: 3p1p:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg250 b:6.5 occ:1.00 O A:HOH253 2.0 19.5 1.0 OE2 A:GLU188 2.2 17.9 1.0 O A:HOH454 2.2 22.6 1.0 CD A:GLU188 3.2 15.6 1.0 CG A:GLU188 3.8 12.5 1.0 OE1 A:GLU188 4.3 17.9 1.0 CB A:GLU188 5.0 10.0 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg251 b:8.7 occ:0.50 OE1 A:GLU2 2.4 16.9 1.0 O A:HOH298 2.5 11.4 1.0 O A:HOH380 2.7 33.7 1.0 CD A:GLU2 3.4 15.9 1.0 OE2 A:GLU2 3.8 15.3 1.0 O A:HOH313 4.1 10.3 1.0 O A:HOH442 4.3 13.3 1.0 CG A:GLU2 4.6 12.6 1.0 CA A:GLU2 4.7 12.1 1.0 N A:ARG3 4.8 11.5 1.0 CB A:GLU2 4.9 11.1 1.0 O A:HOH330 4.9 29.5 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Human 14-3-3 Sigma C38N/N166H in Complex with Task-3 Peptide


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 C38N/N166H in Complex with Task-3 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg252 b:19.9 occ:1.00 O A:HOH261 2.1 39.0 1.0 OE1 A:GLU75 2.2 31.3 1.0 O A:HOH450 2.4 35.8 1.0 CD A:GLU75 3.4 32.1 1.0 CG A:GLU75 4.2 36.5 1.0 O A:HOH393 4.3 41.3 1.0 CB A:GLU75 4.3 38.7 1.0 OE2 A:GLU75 4.3 38.7 1.0 O A:GLY73 4.6 44.0 1.0 CA A:GLU75 4.8 39.7 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