Chlorine in PDB 6bgq: Caspase-3 Mutant - S150D

All present enzymatic activity of Caspase-3 Mutant - S150D:
3.4.22.56;

The structure of Caspase-3 Mutant - S150D, PDB code: 6bgq was solved by M.E.Thomas, R.Grinshpon, P.D.Swartz, A.C.Clark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.65 / 1.97
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.465, 96.210, 68.332, 90.00, 129.01, 90.00
R / Rfree (%)	18 / 22.4

The structure of Caspase-3 Mutant - S150D also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Caspase-3 Mutant - S150D (pdb code 6bgq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Caspase-3 Mutant - S150D, PDB code: 6bgq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Caspase-3 Mutant - S150D


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Caspase-3 Mutant - S150D within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:27.7 occ:1.00 NZ A:LYS53 2.8 25.9 1.0 N A:GLY66 3.0 14.9 1.0 N A:ASP68 3.3 14.4 1.0 CB A:ASP68 3.4 20.4 1.0 CA A:GLY66 3.5 16.8 1.0 N A:THR67 3.5 12.8 1.0 CE A:LYS53 3.6 26.1 1.0 CG A:ASP68 3.6 18.6 1.0 OD2 A:ASP68 3.6 16.2 1.0 C A:GLY66 3.7 13.2 1.0 CA A:ASP68 3.9 11.2 1.0 CD A:LYS53 4.0 11.9 1.0 O A:HOH444 4.1 25.4 1.0 C A:SER65 4.1 16.9 1.0 CA A:SER65 4.3 15.8 1.0 C A:THR67 4.3 11.7 1.0 OD1 A:ASP68 4.3 17.8 1.0 O A:ARG64 4.4 16.9 1.0 CG2 A:THR67 4.4 16.1 1.0 CA A:THR67 4.5 12.3 1.0 CA A:THR67 4.5 12.4 0.0 O A:GLY66 4.5 16.5 1.0 N A:VAL69 4.5 5.8 1.0 OG1 A:THR67 4.5 15.7 0.0 C A:ASP68 4.8 13.6 1.0 CG A:LYS53 5.0 19.8 1.0

Chlorine binding site 2 out of 2 in the Caspase-3 Mutant - S150D


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Caspase-3 Mutant - S150D within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl201 b:31.8 occ:1.00 NZ C:LYS53 2.7 25.9 1.0 N C:GLY66 2.9 17.3 1.0 N C:ASP68 3.3 13.2 1.0 CA C:GLY66 3.5 14.0 1.0 N C:THR67 3.5 11.2 1.0 CB C:ASP68 3.5 15.8 1.0 C C:GLY66 3.6 12.7 1.0 CE C:LYS53 3.7 26.1 1.0 OD2 C:ASP68 3.7 17.7 1.0 CG C:ASP68 3.7 18.0 1.0 C C:SER65 4.0 21.4 1.0 CD C:LYS53 4.0 16.4 1.0 CA C:ASP68 4.0 9.8 1.0 CA C:SER65 4.2 18.9 1.0 O C:ARG64 4.3 15.7 1.0 O C:HOH423 4.3 20.5 1.0 O C:GLY66 4.4 18.5 1.0 C C:THR67 4.4 13.7 1.0 CG2 C:THR67 4.4 13.7 1.0 CA C:THR67 4.5 11.2 1.0 OD1 C:ASP68 4.5 16.9 1.0 N C:VAL69 4.6 7.4 1.0 O C:HOH509 4.7 31.1 1.0 C C:ASP68 4.8 17.0 1.0 CG C:LYS53 4.9 18.2 1.0

M.E.Thomas, R.Grinshpon, P.Swartz, A.C.Clark. Modifications to A Common Phosphorylation Network Provide Individualized Control in Caspases. J. Biol. Chem. V. 293 5447 2018.
ISSN: ESSN 1083-351X
PubMed: 29414778
DOI: 10.1074/JBC.RA117.000728