Brand  (β version)

PDB ID: 1CP3

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
ACE Acetyl group
CF0 Fluoromethane

Structure summary

Code : 1CP3   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : CRYSTAL STRUCTURE OF THE COMPLEX OF APOPAIN WITH THE TETRAPEPTIDE INHIBITOR ACE-DVAD-FMC
Release Data : 1997-12-24
Compound :
mol_id molecule chains synonym
1 APOPAIN A,B CASPASE-3, CPP32, YAMA
ec: 3.4.22.-
mol_id molecule chains
2 ACETYL-ASP-VAL-ALA-ASP-FLUOROMETHYLKETONE C,D
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
mol_id organism_scientific
2
synthetic: yes
Authors : Mittl, P.R.E., Dimarco, S., Gruetter, M.G.
Keywords : HYDROLASE-HYDROLASE INHIBITOR COMPLEX, APOPTOSIS, interleukin-1beta-converting enzyme, CYSTEINE-PROTEASE
Exp. method : X-RAY DIFFRACTION ( 2.3 Å )
Citation :

Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone.

Mittl, P.R.,Di Marco, S.,Krebs, J.F.  et al.
(1997)  J.Biol.Chem.  272 : 6539 - 6547

PubMed: 9045680
DOI: 10.1074/jbc.272.10.6539

Reaction

Chain : A, B
UniProt : P42574 (CASP3_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position. 3.4.22.56 PubMed:16374543, PubMed:18723680, PubMed:20566630, PubMed:23152800, PubMed:23650375, PubMed:23845944, PubMed:30878284, PubMed:33725486, PubMed:7596430
-