Chlorine in PDB 6bh9: Caspase-3 Mutant - T152A

All present enzymatic activity of Caspase-3 Mutant - T152A:
3.4.22.56;

The structure of Caspase-3 Mutant - T152A, PDB code: 6bh9 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)	35.61 / 1.94
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.362, 96.077, 68.212, 90.00, 128.96, 90.00
R / Rfree (%)	14.6 / 18.9

The structure of Caspase-3 Mutant - T152A also contains other interesting chemical elements:

Sodium

(Na)

5 atoms

The binding sites of Chlorine atom in the Caspase-3 Mutant - T152A (pdb code 6bh9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Caspase-3 Mutant - T152A, PDB code: 6bh9:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Caspase-3 Mutant - T152A


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 - T152A within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl6 b:30.0 occ:1.00 CL1 D:0QE6 0.0 30.0 1.0 C1 D:0QE6 1.6 41.0 1.0 C D:ASP5 2.7 41.3 1.0 O D:ASP5 3.1 22.6 1.0 SG B:CYS163 3.3 14.3 1.0 CB B:CYS163 3.7 11.2 1.0 O B:HOH483 3.9 19.3 1.0 CA D:ASP5 4.0 29.8 1.0 CD1 E:TYR204 4.0 14.1 1.0 CE1 E:TYR204 4.0 14.2 1.0 O B:GLY122 4.4 14.2 1.0 N D:ASP5 4.4 25.7 1.0 ND1 B:HIS121 4.6 19.7 1.0 O D:VAL4 4.7 25.9 1.0 C D:VAL4 4.7 26.6 1.0 CG2 D:VAL4 4.8 19.3 1.0

Chlorine binding site 2 out of 4 in the Caspase-3 Mutant - T152A


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 - T152A within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl6 b:30.0 occ:1.00 CL1 G:0QE6 0.0 30.0 1.0 C1 G:0QE6 1.6 41.0 1.0 C G:ASP5 2.5 41.3 1.0 O G:ASP5 2.8 22.6 1.0 SG A:CYS163 2.9 14.2 1.0 CB A:CYS163 3.3 9.9 1.0 CD1 C:TYR204 3.7 15.8 1.0 O A:HOH476 3.8 18.9 1.0 CA G:ASP5 3.8 29.8 1.0 CE1 C:TYR204 3.9 13.1 1.0 N G:ASP5 4.2 25.7 1.0 O A:GLY122 4.3 13.8 1.0 C G:VAL4 4.6 26.6 1.0 CG2 G:VAL4 4.6 19.3 1.0 O G:VAL4 4.7 25.9 1.0 O A:GLY165 4.7 10.9 1.0 ND1 A:HIS121 4.8 20.5 1.0 CA A:CYS163 4.8 10.0 1.0 CB G:VAL4 4.9 18.8 1.0 CB G:ASP5 5.0 24.5 1.0

Chlorine binding site 3 out of 4 in the Caspase-3 Mutant - T152A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Caspase-3 Mutant - T152A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:24.3 occ:1.00 N A:GLY66 3.1 11.0 1.0 NZ A:LYS53 3.2 25.1 1.0 N A:ASP68 3.2 12.0 1.0 CB A:ASP68 3.3 16.6 1.0 CE A:LYS53 3.4 28.2 1.0 N A:THR67 3.5 9.9 1.0 CG A:ASP68 3.6 14.0 1.0 CA A:GLY66 3.6 10.4 1.0 C A:GLY66 3.6 15.2 1.0 OD2 A:ASP68 3.7 15.3 1.0 CA A:ASP68 3.8 12.9 1.0 CD A:LYS53 4.0 17.0 1.0 C A:SER65 4.2 11.8 1.0 C A:THR67 4.2 11.3 1.0 O A:HOH454 4.2 24.9 1.0 OD1 A:ASP68 4.2 13.3 1.0 O A:GLY66 4.3 12.2 1.0 CA A:SER65 4.3 14.2 1.0 N A:VAL69 4.4 8.5 1.0 CA A:THR67 4.4 7.2 1.0 CG2 A:THR67 4.5 11.0 1.0 O A:ARG64 4.5 12.7 1.0 C A:ASP68 4.6 8.9 1.0

Chlorine binding site 4 out of 4 in the Caspase-3 Mutant - T152A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Caspase-3 Mutant - T152A within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl302 b:24.7 occ:1.00 N B:GLY66 3.1 10.3 1.0 N B:ASP68 3.2 14.1 1.0 NZ B:LYS53 3.2 23.3 1.0 CB B:ASP68 3.4 15.3 1.0 CE B:LYS53 3.4 31.4 1.0 N B:THR67 3.5 8.8 1.0 CG B:ASP68 3.6 13.8 1.0 CA B:GLY66 3.6 11.2 1.0 OD2 B:ASP68 3.6 16.0 1.0 C B:GLY66 3.6 13.5 1.0 CA B:ASP68 3.8 13.3 1.0 CD B:LYS53 4.0 10.2 1.0 O B:HOH436 4.1 26.7 1.0 C B:SER65 4.1 13.1 1.0 C B:THR67 4.2 10.3 1.0 CA B:SER65 4.3 18.7 1.0 OD1 B:ASP68 4.3 13.5 1.0 O B:GLY66 4.3 15.8 1.0 CA B:THR67 4.4 8.2 1.0 N B:VAL69 4.4 7.3 1.0 CG2 B:THR67 4.5 11.1 1.0 O B:ARG64 4.5 12.5 1.0 C B:ASP68 4.7 8.8 1.0 CG B:LYS53 4.9 11.0 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