Brand  (β version)

PDB ID: 1RHK

Hetero Atom Contents

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Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
FPR (3s)-3-amino-4-oxo-7-phenylheptanoic acid
Glycosylation
Code Name Emphasize
Modification
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ACE Acetyl group

Structure summary

Code : 1RHK   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystal structure of the complex of caspase-3 with a phenyl-propyl-ketone inhibitor
Release Data : 2004-05-11
Compound :
mol_id molecule chains synonym
1 Caspase-3 A Cysteine protease CPP32, Yama protein, CPP-32, Apopain, CASP-3, SREBP cleavage activity 1, SCA-1
ec: 3.4.22.-
fragment: P17 SUBUNIT
mol_id molecule chains synonym
2 Caspase-3 B Cysteine protease CPP32, Yama protein, CPP-32, Apopain, CASP-3, SREBP cleavage activity 1, SCA-1
ec: 3.4.22.-
fragment: P12 SUBUNIT
mol_id molecule chains
3 acetyl-asp-glu-val-fpr C
other_details: propylbenzene is covalently bound to the C-terminus
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
gene: CASP3, CPP32
expression_system_strain: BL21(DE3)
expression_system_vector_type: PLASMID
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
gene: CASP3, CPP32
expression_system_strain: BL21(DE3)
expression_system_vector_type: PLASMID
mol_id organism_scientific
3
synthetic: yes
other_details: The inhibitor is chemically synthesized.
Authors : Becker, J.W., Rotonda, J., Soisson, S.M.
Keywords : CYSTEINE PROTEASE, CASPASE-3, APOPAIN, CPP32, YAMA, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.50 Å )
Citation :

Reducing the Peptidyl Features of Caspase-3 Inhibitors: A Structural Analysis.

Becker, J.W.,Rotonda, J.,Soisson, S.M.  et al.
(2004)  J.Med.Chem.  47 : 2466 - 2474

PubMed: 15115390
DOI: 10.1021/jm0305523

Reaction

Chain : 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
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