Het-PDB Navi2 (PDB: 1CP3)

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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

Download interaction data: 1CP3

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

Chain :

A, B

UniProt :

P42574 (CASP3_HUMAN)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
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:37993714, PubMed:7596430, PubMed:9334240
	-

PDB ID: 1CP3