Chlorine in PDB 4ehh: Allosteric Modulation of Caspase-3 Through Mutagenesis

All present enzymatic activity of Allosteric Modulation of Caspase-3 Through Mutagenesis:
3.4.22.56;

The structure of Allosteric Modulation of Caspase-3 Through Mutagenesis, PDB code: 4ehh was solved by J.Walters, J.L.Schipper, P.D.Swartz, C.Mattos, A.C.Clark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.01 / 1.78
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	69.024, 84.745, 96.262, 90.00, 90.00, 90.00
R / Rfree (%)	23.8 / 28.1

The binding sites of Chlorine atom in the Allosteric Modulation of Caspase-3 Through Mutagenesis (pdb code 4ehh). 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 Allosteric Modulation of Caspase-3 Through Mutagenesis, PDB code: 4ehh:

Chlorine binding site 1 out of 1 in the Allosteric Modulation of Caspase-3 Through Mutagenesis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Allosteric Modulation of Caspase-3 Through Mutagenesis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl6 b:76.3 occ:1.00 CL1 B:0QE6 0.0 76.3 1.0 C1 B:0QE6 1.7 43.4 1.0 O A:HOH627 2.4 38.6 1.0 C B:ASP5 2.8 35.3 1.0 O B:ASP5 3.0 20.7 1.0 ND1 A:HIS121 3.6 28.2 1.0 CG A:HIS121 4.2 23.6 1.0 CA B:ASP5 4.2 24.3 1.0 CB A:HIS121 4.3 20.0 1.0 O A:GLY122 4.3 18.4 1.0 CE1 A:HIS121 4.4 31.6 1.0 SG A:CYS163 4.4 24.3 1.0 O B:HOH106 4.5 38.6 1.0 CB A:CYS163 4.6 22.9 1.0 N A:GLY122 4.7 21.6 1.0 CA A:HIS121 4.8 23.7 1.0 N B:ASP5 4.8 23.2 1.0 O B:VAL4 4.9 17.4 1.0 O A:HOH552 4.9 27.4 1.0

J.Walters, J.L.Schipper, P.Swartz, C.Mattos, A.C.Clark. Allosteric Modulation of Caspase 3 Through Mutagenesis. Biosci.Rep. V. 32 401 2012.
ISSN: ISSN 0144-8463
PubMed: 22607239
DOI: 10.1042/BSR20120037