Chlorine in PDB 5iab: Caspase 3 V266D

All present enzymatic activity of Caspase 3 V266D:
3.4.22.56;

The structure of Caspase 3 V266D, PDB code: 5iab was solved by J.J.Maciag, S.H.Mackenzie, M.B.Tucker, J.L.Schipper, 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)	33.80 / 1.79
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.590, 96.709, 68.929, 90.00, 126.30, 90.00
R / Rfree (%)	17.3 / 21.3

The binding sites of Chlorine atom in the Caspase 3 V266D (pdb code 5iab). 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 V266D, PDB code: 5iab:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Caspase 3 V266D


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Caspase 3 V266D within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl6 b:26.0 occ:1.00 CL1 D:0QE6 0.0 26.0 1.0 C1 D:0QE6 1.8 49.3 1.0 SG C:CYS163 2.4 69.7 1.0 C D:ASP5 2.5 46.4 1.0 CB C:CYS163 2.9 21.0 1.0 CA C:CYS163 3.0 12.1 1.0 O D:ASP5 3.2 47.4 1.0 N D:ASP5 3.2 31.1 1.0 N C:SER205 3.3 12.4 1.0 CA D:ASP5 3.3 44.1 1.0 N C:CYS163 3.3 12.8 1.0 CB D:ASP5 3.4 37.5 1.0 O C:SER205 3.7 19.0 1.0 CD1 C:TYR204 3.8 22.6 1.0 CA C:TYR204 3.8 12.8 1.0 C C:TYR204 4.1 11.0 1.0 CB C:TYR204 4.2 16.9 1.0 O C:HOH407 4.2 32.6 1.0 C D:VAL4 4.2 32.7 1.0 CA C:SER205 4.2 11.7 1.0 O D:HOH201 4.3 31.9 1.0 CB C:SER205 4.4 12.5 1.0 C C:SER205 4.4 11.3 1.0 C C:ALA162 4.4 13.8 1.0 CG C:TYR204 4.5 16.3 1.0 C C:CYS163 4.5 11.8 1.0 CB D:VAL4 4.5 19.4 1.0 O C:GLY165 4.7 16.8 1.0 CA D:VAL4 4.7 19.2 1.0 CE1 C:TYR204 4.8 21.3 1.0 CG D:ASP5 4.9 38.8 1.0 O D:VAL4 5.0 38.1 1.0

Chlorine binding site 2 out of 2 in the Caspase 3 V266D


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Caspase 3 V266D within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl6 b:74.8 occ:1.00 CL1 E:0QE6 0.0 74.8 1.0 C1 E:0QE6 1.8 38.1 1.0 SG A:CYS163 2.6 57.5 1.0 C E:ASP5 2.7 49.6 1.0 N A:SER205 2.9 10.4 1.0 N E:ASP5 2.9 29.8 1.0 CD1 A:TYR204 3.1 20.5 1.0 CA A:TYR204 3.2 10.3 1.0 CB A:CYS163 3.3 17.6 1.0 O A:SER205 3.3 19.6 1.0 CA E:ASP5 3.4 42.5 1.0 CB A:TYR204 3.4 17.3 1.0 O E:ASP5 3.5 39.1 1.0 C A:TYR204 3.5 11.2 1.0 CA A:CYS163 3.7 11.8 1.0 CG A:TYR204 3.7 15.3 1.0 C E:VAL4 3.8 41.1 1.0 CB E:VAL4 3.9 15.8 1.0 CA A:SER205 3.9 11.0 1.0 C A:SER205 4.0 14.3 1.0 CB E:ASP5 4.1 46.1 1.0 N A:CYS163 4.1 13.2 1.0 CE1 A:TYR204 4.2 24.6 1.0 CA E:VAL4 4.3 20.1 1.0 CB A:SER205 4.4 13.9 1.0 N A:TYR204 4.6 11.1 1.0 O E:VAL4 4.7 34.8 1.0 CG1 E:VAL4 4.7 21.7 1.0 O A:GLY165 4.7 17.0 1.0 O A:TYR204 4.8 15.0 1.0 CG2 E:VAL4 4.8 30.1 1.0 O A:TYR203 5.0 11.3 1.0

J.J.Maciag, S.H.Mackenzie, M.B.Tucker, J.L.Schipper, P.Swartz, A.C.Clark. Tunable Allosteric Library of Caspase-3 Identifies Coupling Between Conserved Water Molecules and Conformational Selection. Proc.Natl.Acad.Sci.Usa V. 113 E6080 2016.
ISSN: ESSN 1091-6490
PubMed: 27681633
DOI: 10.1073/PNAS.1603549113