Calcium 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:

Magnesium	(Mg)	4 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Human 14-3-3 Sigma C38V/N166H in Complex with Task-3 Peptide, PDB code: 3p1r:

Calcium binding site 1 out of 1 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 Calcium with other atoms in the Ca 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:Ca256 b:11.9 occ:1.00 O A:HOH483 2.3 18.1 1.0 OE2 A:GLU188 2.4 14.0 1.0 CD A:GLU188 3.4 12.5 1.0 CG A:GLU188 3.8 7.5 1.0 O A:HOH506 4.2 32.6 1.0 OE1 A:GLU188 4.5 12.1 1.0 O A:HOH432 4.6 15.9 1.0 O A:HOH471 4.8 23.0 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