Chlorine in PDB 7obg: Crystal Structure of 14-3-3 Sigma in Complex with NPM1 Phosphopeptide

The structure of Crystal Structure of 14-3-3 Sigma in Complex with NPM1 Phosphopeptide, PDB code: 7obg was solved by F.Centorrino, B.Andlovic, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.09 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.65, 112.265, 62.65, 90, 90, 90
R / Rfree (%)	14.4 / 17.4

The structure of Crystal Structure of 14-3-3 Sigma in Complex with NPM1 Phosphopeptide also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Chlorine atom in the Crystal Structure of 14-3-3 Sigma in Complex with NPM1 Phosphopeptide (pdb code 7obg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of 14-3-3 Sigma in Complex with NPM1 Phosphopeptide, PDB code: 7obg:

Chlorine binding site 1 out of 1 in the Crystal Structure of 14-3-3 Sigma in Complex with NPM1 Phosphopeptide


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 14-3-3 Sigma in Complex with NPM1 Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:8.7 occ:1.00 HZ3 A:LYS9 2.2 8.2 1.0 HD3 A:LYS9 3.0 5.5 1.0 NZ A:LYS9 3.1 6.8 1.0 HZ2 A:LYS9 3.4 8.2 1.0 HZ A:PHE25 3.5 6.3 1.0 HZ1 A:LYS9 3.6 8.2 1.0 CD A:LYS9 3.7 4.6 1.0 CE A:LYS9 3.8 4.5 1.0 HE1 A:MET1 3.8 12.3 1.0 HE2 A:LYS9 3.8 5.5 1.0 HE2 A:PHE25 4.0 7.0 1.0 HD2 A:LYS9 4.1 5.5 1.0 CZ A:PHE25 4.2 5.2 1.0 HE2 A:MET1 4.3 12.3 1.0 CE A:MET1 4.5 10.2 1.0 CE2 A:PHE25 4.5 5.8 1.0 HE3 A:LYS9 4.7 5.5 1.0 O A:HOH773 4.9 29.1 1.0 HG2 A:LYS9 5.0 4.6 1.0 CG A:LYS9 5.0 3.8 1.0

B.Andlovic, G.Heilmann, S.Ninck, S.Andrei, F.Centorrino, Y.Higuchi, N.Kato, L.Brunsveld, S.Menninger, A.Choidas, A.Wolf, M.Kaiser, J.Eickhoff, C.Ottmann. Inf Alpha Primes Ovarian Cancer Cells For Fusicoccin-Induced Cell Death Via Stabilization of 14-3-3 Protein-Protein Interactions To Be Published.