Chlorine 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
Calcium	(Ca)	1 atom

The binding sites of Chlorine 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 Chlorine atom.
In total 4 binding sites of Chlorine 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 Chlorine binding site number: 1; 2; 3; 4;

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl252 b:12.3 occ:1.00 O A:HOH456 2.9 19.6 1.0 O A:HOH478 3.1 16.4 1.0 CD A:LYS87 3.6 12.2 0.5 CA A:TYR84 3.8 7.3 1.0 O A:GLU83 3.9 5.7 1.0 CB A:LYS87 4.0 8.1 0.5 CB A:LYS87 4.0 8.2 0.5 CD1 A:TYR84 4.0 7.8 1.0 C A:GLU83 4.0 7.0 1.0 N A:TYR84 4.0 5.3 1.0 CB A:TYR84 4.2 5.7 1.0 CB A:GLU83 4.3 7.7 1.0 CD A:LYS87 4.3 13.3 0.5 CG A:LYS87 4.4 11.8 0.5 CG A:LYS87 4.5 11.9 0.5 O A:HOH411 4.5 16.3 1.0 CG A:TYR84 4.5 7.1 1.0 CE A:LYS87 4.8 15.5 0.5 CA A:GLU83 4.8 6.9 1.0 O A:HOH464 5.0 39.1 1.0

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl253 b:51.8 occ:1.00 OE2 A:GLU153 2.5 17.4 0.4 O A:HOH409 2.7 15.0 1.0 NZ A:LYS124 3.3 13.9 1.0 CD A:GLU153 3.5 20.1 0.4 CA A:ALA150 3.6 6.8 1.0 CE A:LYS124 3.7 12.5 1.0 N A:ALA150 3.8 5.4 1.0 CD A:LYS124 3.8 7.5 1.0 CB A:ALA150 3.9 5.4 1.0 OE1 A:GLU153 4.0 23.0 0.4 OG A:SER149 4.1 16.4 1.0 C A:SER149 4.2 8.8 1.0 O A:SER149 4.4 8.0 1.0 OE1 A:GLU153 4.4 16.2 0.6 CD2 A:LEU121 4.5 8.4 1.0 CB A:SER149 4.6 11.6 1.0 CG A:GLU153 4.7 11.5 0.4 O A:HOH459 4.9 52.4 1.0 O A:SER146 4.9 6.8 1.0 CG A:LYS124 5.0 4.1 1.0

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl254 b:47.3 occ:1.00 O A:HOH499 2.4 20.0 1.0 O A:HOH367 3.0 8.0 1.0 N A:GLU20 3.4 6.8 1.0 N A:TYR19 3.5 6.0 1.0 CG A:GLU20 3.7 7.1 0.5 CB A:GLU20 3.8 7.9 0.5 CB A:GLU20 3.9 7.8 0.5 C A:ARG18 4.0 7.2 1.0 CA A:ARG18 4.1 7.7 1.0 CD A:GLU20 4.2 20.1 0.5 CA A:GLU20 4.2 7.5 0.5 CA A:GLU20 4.3 7.3 0.5 CA A:TYR19 4.3 6.2 1.0 OE1 A:GLU20 4.3 24.2 0.5 C A:TYR19 4.3 5.8 1.0 O A:GLU17 4.3 12.2 1.0 O A:HOH497 4.4 25.1 1.0 O A:HOH495 4.7 25.6 1.0 CB A:TYR19 4.7 6.9 1.0 O A:ARG18 4.9 6.8 1.0 OE2 A:GLU20 5.0 18.4 0.5

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl255 b:43.0 occ:1.00 O A:HOH277 2.6 38.3 1.0 O A:THR228 2.6 11.1 1.0 OXT A:THR231 2.8 22.4 1.0 O A:HOH291 3.0 38.7 1.0 C A:THR231 3.6 21.9 1.0 C A:THR228 3.6 11.8 1.0 CG2 A:THR228 3.9 14.4 1.0 O A:THR231 4.0 24.9 1.0 CA A:THR228 4.1 11.5 1.0 CA A:THR231 4.6 18.8 1.0 N A:THR231 4.6 14.9 1.0 CB A:THR228 4.7 12.0 1.0 OG1 A:THR231 4.8 18.3 1.0 N A:LEU229 4.8 10.7 1.0 O A:LEU227 5.0 9.5 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