Magnesium in PDB 3p1r: Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide

The structure of Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide, PDB code: 3p1r 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)	19.58 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.320, 112.290, 62.690, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 19.4

The structure of Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Chlorine	(Cl)	4 atoms

The binding sites of Magnesium atom in the Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide (pdb code 3p1r). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide, PDB code: 3p1r:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of Human 14-3-3 Sigma C38V/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 C38V/N166H in Complex with Task-3 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg249 b:13.7 occ:1.00 OE1 A:GLU75 2.3 21.8 1.0 O A:HOH536 2.4 24.7 1.0 O A:HOH309 2.5 38.4 1.0 CD A:GLU75 3.5 23.6 1.0 CG A:GLU75 4.2 28.5 1.0 OE2 A:GLU75 4.4 25.1 1.0 CB A:GLU75 4.5 29.2 1.0 O A:GLY73 4.7 37.5 1.0 CA A:GLU75 4.9 29.1 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of Human 14-3-3 Sigma C38V/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 C38V/N166H in Complex with Task-3 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg250 b:3.9 occ:0.50 O A:HOH364 2.2 38.0 1.0 OE1 A:GLU2 2.3 11.6 1.0 O A:HOH283 2.6 2.0 0.5 O A:HOH365 2.6 41.1 1.0 CD A:GLU2 3.3 9.5 1.0 OE2 A:GLU2 3.7 10.0 1.0 O A:HOH396 4.1 9.1 1.0 O A:HOH378 4.6 10.6 1.0 O A:HOH303 4.6 31.7 1.0 CG A:GLU2 4.6 8.3 1.0 CA A:GLU2 4.8 7.8 1.0 O A:HOH412 4.8 16.7 1.0 CB A:GLU2 4.9 7.1 1.0 N A:ARG3 4.9 6.5 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of Human 14-3-3 Sigma C38V/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 C38V/N166H in Complex with Task-3 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg251 b:26.9 occ:1.00 O A:HOH300 2.7 40.4 1.0 O A:ASP215 2.8 9.5 1.0 O A:HOH496 3.0 27.2 1.0 O A:HOH268 3.4 51.0 1.0 CD2 A:LEU218 3.5 11.1 0.5 C A:ASP215 3.6 9.3 1.0 CA A:ASP215 3.6 10.0 1.0 CG1 A:ILE219 3.6 9.9 0.5 CD1 A:ILE219 3.6 10.9 0.5 CG1 A:ILE219 3.9 7.7 0.5 CB A:LEU218 3.9 9.8 0.5 CB A:ASP215 4.0 11.1 1.0 CD1 A:ILE219 4.0 3.5 0.5 CB A:LEU218 4.1 10.2 0.5 CG A:LEU218 4.2 12.0 0.5 CD2 A:LEU218 4.3 17.5 0.5 OD1 A:ASP215 4.4 18.5 1.0 CG A:LEU218 4.5 14.3 0.5 O A:HOH579 4.6 24.1 1.0 CG A:ASP215 4.6 15.5 1.0 CD1 A:LEU218 4.7 14.2 0.5 CB A:PRO167 4.7 4.5 1.0 CG A:PRO167 4.8 8.3 1.0 N A:SER216 4.8 6.3 1.0 N A:ILE219 4.8 7.9 1.0 O A:LYS214 4.9 10.8 1.0 N A:ASP215 5.0 8.8 1.0 O P:HOH295 5.0 29.0 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of Human 14-3-3 Sigma C38V/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 4 of Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg257 b:19.7 occ:1.00 O A:HOH538 2.4 27.1 1.0 OE1 A:GLN8 2.4 15.4 0.4 NE2 A:GLN8 2.7 10.9 0.6 CD A:GLN8 3.2 12.1 0.4 NE2 A:GLN8 3.2 16.5 0.4 CD A:GLN8 3.8 5.7 0.6 OE1 A:GLN8 4.0 7.6 0.6 O A:HOH421 4.4 15.1 1.0 CG A:GLN8 4.7 5.7 0.4 OG A:SER5 4.8 6.2 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