Copper in PDB 4fea: Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor

All present enzymatic activity of Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor:
3.4.22.60;

The structure of Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor, PDB code: 4fea was solved by V.Kabaleeswaran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.83 / 3.79
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.720, 88.720, 185.660, 90.00, 90.00, 120.00
R / Rfree (%)	23.6 / 28.6

The structure of Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Copper atom in the Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor (pdb code 4fea). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor, PDB code: 4fea:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu701 b:1.0 occ:1.00 CU1 A:0TE701 0.0 1.0 1.0 N3 A:0TE701 2.0 0.0 1.0 N1 A:0TE701 2.1 0.9 1.0 S1 A:0TE701 2.2 0.5 1.0 CL1 A:0TE701 2.3 0.4 1.0 SG A:CYS290 2.8 95.5 1.0 C6 A:0TE701 2.9 0.3 1.0 C5 A:0TE701 2.9 0.6 1.0 N4 A:0TE701 3.0 0.8 1.0 C12 A:0TE701 3.0 0.6 1.0 C1 A:0TE701 3.1 0.1 1.0 CB A:CYS290 3.5 90.3 1.0 C4 A:0TE701 4.3 0.6 1.0 C2 A:0TE701 4.4 0.3 1.0 C7 A:0TE701 4.4 0.8 1.0 N A:CYS290 4.7 0.7 1.0 CA A:CYS290 4.7 99.8 1.0 S2 A:0TE701 4.8 0.4 1.0 C3 A:0TE701 4.8 0.1 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Caspase-7 in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu701 b:0.1 occ:1.00 CU1 B:0TE701 0.0 0.1 1.0 N3 B:0TE701 2.0 0.9 1.0 N1 B:0TE701 2.1 0.4 1.0 S1 B:0TE701 2.2 0.5 1.0 CL1 B:0TE701 2.3 0.1 1.0 SG B:CYS290 2.8 0.1 1.0 C6 B:0TE701 2.9 0.9 1.0 C5 B:0TE701 2.9 0.4 1.0 C12 B:0TE701 3.0 0.8 1.0 N4 B:0TE701 3.0 0.5 1.0 C1 B:0TE701 3.1 0.7 1.0 C4 B:0TE701 4.3 0.5 1.0 C7 B:0TE701 4.4 0.4 1.0 C2 B:0TE701 4.4 0.7 1.0 CB B:CYS290 4.5 0.2 1.0 S2 B:0TE701 4.8 0.1 1.0 C3 B:0TE701 4.8 0.8 1.0 CB B:TYR223 4.9 69.7 1.0

T.Feldman, V.Kabaleeswaran, S.B.Jang, C.Antczak, H.Djaballah, H.Wu, X.Jiang. A Class of Allosteric Caspase Inhibitors Identified By High-Throughput Screening. Mol.Cell V. 47 585 2012.
ISSN: ISSN 1097-2765
PubMed: 22795132
DOI: 10.1016/J.MOLCEL.2012.06.007