Chlorine in PDB 5iae: Caspase 3 V266F

All present enzymatic activity of Caspase 3 V266F:
3.4.22.56;

The structure of Caspase 3 V266F, PDB code: 5iae 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)	23.98 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.223, 68.765, 84.706, 90.00, 131.34, 90.00
R / Rfree (%)	15.5 / 18.2

The binding sites of Chlorine atom in the Caspase 3 V266F (pdb code 5iae). 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 V266F, PDB code: 5iae:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Caspase 3 V266F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Caspase 3 V266F within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:21.8 occ:1.00 N A:GLY66 3.1 10.5 1.0 NZ A:LYS53 3.2 31.7 1.0 N A:ASP68 3.3 11.2 1.0 CB A:ASP68 3.5 11.0 1.0 CE A:LYS53 3.5 27.7 1.0 N A:THR67 3.6 9.1 1.0 CG A:ASP68 3.6 17.9 1.0 OD2 A:ASP68 3.7 15.9 1.0 CA A:GLY66 3.7 9.7 1.0 C A:GLY66 3.7 11.1 1.0 CA A:ASP68 3.9 11.9 1.0 CD A:LYS53 4.0 16.9 1.0 O A:HOH445 4.1 27.9 1.0 C A:SER65 4.1 10.6 1.0 CA A:SER65 4.2 12.9 1.0 OD1 A:ASP68 4.3 15.1 1.0 C A:THR67 4.3 11.0 1.0 O A:ARG64 4.4 11.1 1.0 CA A:THR67 4.5 10.0 1.0 O A:GLY66 4.5 12.9 1.0 CG2 A:THR67 4.5 10.6 1.0 O A:HOH636 4.6 33.9 1.0 N A:VAL69 4.6 11.2 1.0 C A:ASP68 4.8 9.8 1.0 CG A:LYS53 4.9 11.6 1.0

Chlorine binding site 2 out of 2 in the Caspase 3 V266F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Caspase 3 V266F within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl301 b:21.6 occ:1.00 NZ C:LYS53 3.1 27.9 1.0 N C:GLY66 3.1 11.5 1.0 N C:ASP68 3.2 10.5 1.0 CB C:ASP68 3.4 10.2 1.0 CE C:LYS53 3.5 23.2 1.0 N C:THR67 3.6 8.5 1.0 CG C:ASP68 3.6 18.6 1.0 CA C:GLY66 3.7 11.2 1.0 OD2 C:ASP68 3.7 15.1 1.0 C C:GLY66 3.7 12.0 1.0 CA C:ASP68 3.9 11.4 1.0 CD C:LYS53 4.0 17.5 1.0 O C:HOH455 4.1 27.1 1.0 C C:SER65 4.1 10.7 1.0 C C:THR67 4.3 10.2 1.0 OD1 C:ASP68 4.3 15.7 1.0 CA C:SER65 4.3 12.8 1.0 O C:HOH658 4.4 35.9 1.0 O C:GLY66 4.4 12.0 1.0 O C:ARG64 4.4 10.9 1.0 CA C:THR67 4.4 8.5 1.0 CG2 C:THR67 4.5 8.8 1.0 N C:VAL69 4.5 11.3 1.0 C C:ASP68 4.8 10.4 1.0 CG C:LYS53 5.0 11.8 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