Chlorine in PDB 6bg4: Caspase-3 Mutant- T152D

All present enzymatic activity of Caspase-3 Mutant- T152D:
3.4.22.56;

The structure of Caspase-3 Mutant- T152D, PDB code: 6bg4 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)	36.31 / 1.87
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	109.209, 96.685, 68.626, 90.00, 126.76, 90.00
R / Rfree (%)	16.4 / 20.7

The structure of Caspase-3 Mutant- T152D also contains other interesting chemical elements:

Sodium

(Na)

13 atoms

The binding sites of Chlorine atom in the Caspase-3 Mutant- T152D (pdb code 6bg4). 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- T152D, PDB code: 6bg4:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Caspase-3 Mutant- T152D


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- T152D within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl6 b:30.0 occ:1.00 CL1 C:0QE6 0.0 30.0 1.0 C1 C:0QE6 1.9 41.0 1.0 C C:ASP5 3.0 41.3 1.0 O C:ASP5 3.4 22.6 1.0 SG A:CYS163 3.4 14.1 1.0 O A:HOH460 3.6 16.1 1.0 CB A:CYS163 3.6 12.6 1.0 CE1 E:TYR204 3.6 17.3 1.0 CD1 E:TYR204 3.8 14.7 1.0 O A:GLY122 4.2 15.8 1.0 CA C:ASP5 4.4 29.8 1.0 O A:GLY165 4.4 15.0 1.0 O C:HOH103 4.6 30.7 1.0 ND1 A:HIS121 4.6 20.0 0.7 ND1 A:HIS121 4.7 19.9 0.3 N C:ASP5 4.7 25.7 1.0 CZ E:TYR204 4.9 21.0 1.0 CG2 A:THR166 4.9 15.9 1.0

Chlorine binding site 2 out of 4 in the Caspase-3 Mutant- T152D


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- T152D 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 1.8 41.0 1.0 C D:ASP5 2.7 41.3 1.0 O D:ASP5 3.0 22.6 1.0 SG B:CYS163 3.3 12.5 1.0 CB B:CYS163 3.5 9.8 1.0 O B:HOH363 3.6 17.4 1.0 CE1 F:TYR204 3.7 14.7 1.0 CD1 F:TYR204 3.7 13.0 1.0 CA D:ASP5 4.1 29.8 1.0 O B:GLY122 4.3 12.5 1.0 N D:ASP5 4.4 25.7 1.0 ND1 B:HIS121 4.5 20.8 1.0 O B:GLY165 4.5 12.9 1.0 O D:VAL4 4.8 25.9 1.0 CG2 D:VAL4 4.8 19.3 1.0 C D:VAL4 4.8 26.6 1.0

Chlorine binding site 3 out of 4 in the Caspase-3 Mutant- T152D


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- T152D within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:24.0 occ:1.00 N A:GLY66 3.1 13.9 1.0 NZ A:LYS53 3.2 29.6 1.0 N A:ASP68 3.2 16.5 1.0 CB A:ASP68 3.4 18.1 1.0 CE A:LYS53 3.5 30.0 1.0 N A:THR67 3.5 14.9 1.0 CA A:GLY66 3.6 15.0 1.0 CG A:ASP68 3.6 21.5 1.0 C A:GLY66 3.6 17.1 1.0 OD2 A:ASP68 3.7 19.4 1.0 CA A:ASP68 3.9 12.3 1.0 CD A:LYS53 4.0 21.4 1.0 C A:SER65 4.1 17.1 1.0 OD1 A:ASP68 4.2 19.1 1.0 C A:THR67 4.2 14.5 1.0 CA A:SER65 4.3 19.3 1.0 O A:ARG64 4.4 13.1 1.0 CA A:THR67 4.4 16.0 1.0 O A:GLY66 4.4 15.8 1.0 O A:HOH445 4.4 33.2 1.0 CG2 A:THR67 4.5 15.3 1.0 N A:VAL69 4.5 14.0 1.0 C A:ASP68 4.7 15.5 1.0 CG A:LYS53 4.9 18.0 1.0

Chlorine binding site 4 out of 4 in the Caspase-3 Mutant- T152D


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- T152D within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl204 b:25.8 occ:1.00 N B:GLY66 3.0 15.7 1.0 NZ B:LYS53 3.2 32.2 1.0 N B:ASP68 3.2 12.5 1.0 CB B:ASP68 3.4 19.6 1.0 CE B:LYS53 3.5 31.0 1.0 CG B:ASP68 3.5 23.4 1.0 CA B:GLY66 3.6 13.8 1.0 N B:THR67 3.6 12.8 1.0 OD2 B:ASP68 3.6 22.0 1.0 C B:GLY66 3.7 14.5 1.0 CA B:ASP68 3.9 15.1 1.0 C B:SER65 4.1 13.9 1.0 CD B:LYS53 4.1 20.3 1.0 O B:HOH354 4.2 29.3 1.0 OD1 B:ASP68 4.2 16.4 1.0 CA B:SER65 4.2 18.9 1.0 C B:THR67 4.3 17.4 1.0 O B:GLY66 4.4 16.7 1.0 N B:VAL69 4.5 13.7 1.0 CA B:THR67 4.5 15.3 1.0 O B:ARG64 4.5 14.2 1.0 CG2 B:THR67 4.5 15.2 1.0 C B:ASP68 4.7 12.1 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