Chlorine in PDB 3pd1: Caspase-3 K242A

All present enzymatic activity of Caspase-3 K242A:
3.4.22.56;

The structure of Caspase-3 K242A, PDB code: 3pd1 was solved by J.Walters, P.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)	33.71 / 1.62
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.670, 84.530, 96.170, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 22.6

The binding sites of Chlorine atom in the Caspase-3 K242A (pdb code 3pd1). 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 Caspase-3 K242A, PDB code: 3pd1:

Chlorine binding site 1 out of 1 in the Caspase-3 K242A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Caspase-3 K242A within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl6 b:21.7 occ:0.05 CL1 B:0QE6 0.0 21.7 0.1 C1 B:0QE6 1.8 22.4 1.0 C B:ASP5 2.8 20.1 1.0 O B:VAL4 2.8 17.1 1.0 O A:HOH468 2.8 52.4 1.0 O A:HOH378 2.9 36.3 1.0 C B:VAL4 3.1 16.4 1.0 CA B:ASP5 3.3 18.9 1.0 N B:ASP5 3.4 16.5 1.0 CG2 B:VAL4 3.4 17.3 1.0 O B:ASP5 3.8 17.2 1.0 ND1 A:HIS121 4.0 18.2 1.0 CB B:VAL4 4.0 16.4 1.0 CE1 A:HIS121 4.1 18.4 1.0 CA B:VAL4 4.2 15.2 1.0 SG A:CYS163 4.3 14.0 1.0 O A:HOH344 4.4 34.5 1.0 CE1 A:TYR204 4.5 16.2 1.0 CD1 A:TYR204 4.7 13.6 1.0 CB B:ASP5 4.8 17.3 1.0 O A:HOH370 4.8 37.3 1.0 O A:HOH368 4.8 27.1 1.0 O A:HOH369 4.9 30.1 1.0 N B:VAL4 4.9 16.4 1.0

J.Walters, P.Swartz, C.Mattos, A.C.Clark. Thermodynamic, Enzymatic and Structural Effects of Removing A Salt Bridge at the Base of Loop 4 in (Pro)Caspase-3. Arch.Biochem.Biophys. V. 508 31 2011.
ISSN: ISSN 0003-9861
PubMed: 21266160
DOI: 10.1016/J.ABB.2011.01.011