Chlorine in PDB 4jr1: Human Procaspase-7 Bound to Ac-Devd-Cmk

All present enzymatic activity of Human Procaspase-7 Bound to Ac-Devd-Cmk:
3.4.22.60;

The structure of Human Procaspase-7 Bound to Ac-Devd-Cmk, PDB code: 4jr1 was solved by N.D.Thomsen, J.A.Wells, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.71 / 2.15
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	57.284, 100.016, 161.587, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 22.7

The binding sites of Chlorine atom in the Human Procaspase-7 Bound to Ac-Devd-Cmk (pdb code 4jr1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Procaspase-7 Bound to Ac-Devd-Cmk, PDB code: 4jr1:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Procaspase-7 Bound to Ac-Devd-Cmk


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Procaspase-7 Bound to Ac-Devd-Cmk within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:56.8 occ:1.00 N A:GLY89 2.8 32.6 1.0 NZ A:LYS76 3.3 38.3 1.0 CA A:GLY89 3.4 31.7 1.0 N A:ASP91 3.4 30.7 1.0 CB A:ASP91 3.4 38.4 1.0 OD2 A:ASP91 3.5 38.8 1.0 N A:THR90 3.5 25.4 1.0 CE A:LYS76 3.6 35.5 1.0 C A:GLY89 3.6 27.0 1.0 CG A:ASP91 3.7 39.2 1.0 C A:ASN88 3.8 33.3 1.0 O A:HOH540 3.8 42.0 1.0 CA A:ASP91 4.0 32.1 1.0 CA A:ASN88 4.0 34.6 1.0 CD A:LYS76 4.2 26.6 1.0 O A:ARG87 4.4 26.7 1.0 C A:THR90 4.4 29.3 1.0 O A:GLY89 4.5 31.8 1.0 CA A:THR90 4.5 26.5 1.0 N A:LYS92 4.6 29.8 1.0 OD1 A:ASP91 4.7 40.9 1.0 CG2 A:THR90 4.7 26.1 1.0 CB A:ASN88 4.8 36.1 1.0 C A:ASP91 4.8 29.3 1.0 OD1 A:ASN88 4.9 39.4 1.0 O A:ASN88 4.9 32.9 1.0

Chlorine binding site 2 out of 2 in the Human Procaspase-7 Bound to Ac-Devd-Cmk


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Procaspase-7 Bound to Ac-Devd-Cmk within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl401 b:40.1 occ:1.00 N B:GLY89 2.7 35.6 1.0 OD2 B:ASP91 3.2 49.9 1.0 NZ B:LYS76 3.3 35.1 1.0 N B:ASP91 3.4 34.2 1.0 CE B:LYS76 3.4 36.0 1.0 N B:THR90 3.5 32.0 1.0 CB B:ASP91 3.5 40.4 1.0 CA B:GLY89 3.6 29.4 1.0 CG B:ASP91 3.6 45.8 1.0 C B:ASN88 3.6 36.9 1.0 CA B:ASN88 3.7 37.5 1.0 C B:GLY89 3.8 32.6 1.0 CD B:LYS76 3.9 32.8 1.0 O B:ARG87 4.1 37.4 1.0 CA B:ASP91 4.1 35.7 1.0 CG2 B:THR90 4.4 26.0 1.0 OD1 B:ASN88 4.4 46.2 1.0 C B:THR90 4.4 31.3 1.0 CA B:THR90 4.5 30.4 1.0 CB B:ASN88 4.5 40.7 1.0 OD1 B:ASP91 4.5 46.0 1.0 N B:ASN88 4.7 36.4 1.0 O B:GLY89 4.7 27.3 1.0 CG B:LYS76 4.8 32.2 1.0 C B:ARG87 4.8 35.0 1.0 O B:ASN88 4.8 29.1 1.0 CG B:ASN88 4.8 44.6 1.0 N B:LYS92 4.9 35.8 1.0

N.D.Thomsen, J.T.Koerber, J.A.Wells. Structural Snapshots Reveal Distinct Mechanisms of Procaspase-3 and -7 Activation. Proc.Natl.Acad.Sci.Usa V. 110 8477 2013.
ISSN: ISSN 0027-8424
PubMed: 23650375
DOI: 10.1073/PNAS.1306759110