Chlorine in PDB 4ehk: 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: 4ehk 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)	27.48 / 1.67
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	109.820, 96.775, 69.176, 90.00, 127.39, 90.00
R / Rfree (%)	19.6 / 23

The binding sites of Chlorine atom in the Allosteric Modulation of Caspase-3 Through Mutagenesis (pdb code 4ehk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Allosteric Modulation of Caspase-3 Through Mutagenesis, PDB code: 4ehk:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 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:35.7 occ:1.00 CL1 B:0QE6 0.0 35.7 1.0 C1 B:0QE6 1.7 27.4 1.0 O A:HOH601 2.8 42.7 1.0 C B:ASP5 2.8 34.9 1.0 O B:ASP5 3.1 21.1 1.0 SG A:CYS163 3.4 18.5 1.0 CB A:CYS163 3.7 15.2 1.0 O A:HOH453 3.8 27.3 1.0 CE1 A:TYR204 3.8 23.1 1.0 CD1 A:TYR204 3.9 18.1 1.0 CA B:ASP5 4.1 19.5 1.0 N B:ASP5 4.4 15.8 1.0 O A:GLY122 4.4 18.8 1.0 O B:HOH109 4.5 37.5 1.0 ND1 A:HIS121 4.5 27.6 1.0 CG2 B:VAL4 4.8 20.5 1.0 C B:VAL4 4.8 20.9 1.0 O A:GLY165 4.8 19.7 1.0 O B:VAL4 4.9 18.7 1.0

Chlorine binding site 2 out of 2 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 2 of Allosteric Modulation of Caspase-3 Through Mutagenesis within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl6 b:35.2 occ:1.00 CL1 D:0QE6 0.0 35.2 1.0 C1 D:0QE6 1.8 29.9 1.0 O C:HOH513 2.5 52.6 1.0 C D:ASP5 2.8 31.9 1.0 O D:ASP5 3.1 21.5 1.0 SG C:CYS163 3.4 15.7 0.8 CB C:CYS163 3.6 17.8 1.0 O C:HOH438 3.7 24.5 1.0 CE1 C:TYR204 3.8 23.8 1.0 CD1 C:TYR204 3.9 18.2 1.0 O C:GLY122 4.2 21.2 1.0 CA D:ASP5 4.2 17.9 1.0 N D:ASP5 4.5 16.9 1.0 ND1 C:HIS121 4.5 26.0 1.0 O C:GLY165 4.8 21.9 1.0 C D:VAL4 5.0 21.6 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