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Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
ASA Aspartic aldehyde
Glycosylation
Code Name Emphasize
Modification
Code Name Show
PHQ Benzyl chlorocarbonate
Code : 1F9E   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : CASPASE-8 SPECIFICITY PROBED AT SUBSITE S4: CRYSTAL STRUCTURE OF THE CASPASE-8-Z-DEVD-CHO
Release Data : 2001-07-10
Compound :
mol_id molecule chains
1 CASPASE-8 ALPHA CHAIN A,C,E,G,I,K
ec: 3.4.22.-
mol_id molecule chains
2 CASPASE-8 BETA CHAIN B,D,F,H,J,L
mol_id molecule chains
3 (PHQ)DEVD Q,R,S,T,U,V
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
expression_system_vector_type: PLASMID
expression_system_plasmid: PET21B
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
expression_system_vector_type: PLASMID
expression_system_plasmid: PET21B
mol_id organism_scientific
3
synthetic: yes
other_details: chemically synthesized
Authors : Blanchard, H., Donepudi, M., Tschopp, M., Kodandapani, L., Wu, J.C., Grutter, M.G.
Keywords : CYSTEINE PROTEASE, CASPASE-8, FLICE, MCH5, MACH, APOPTOSIS, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.9 Å )
Citation :

Caspase-8 specificity probed at subsite S(4): crystal structure of the caspase-8-Z-DEVD-cho complex.

Blanchard, H.,Donepudi, M.,Tschopp, M.  et al.
(2000)  J.Mol.Biol.  302 : 9 - 16

PubMed: 10964557
DOI: 10.1006/jmbi.2000.4041

The three-dimensional structure of caspase-8: an initiator enzyme in apoptosis

Blanchard, H.,Kodandapani, L.,Mittl, P.R.E.  et al.
(1999)  Structure  7 : 1125 - 1133

DOI: 10.1016/S0969-2126(99)80179-8

The atomic-resolution of human caspase-8, a key activator of apoptosis.

Watt, W.,Koeplinger, K.A.,Mildner, A.M.  et al.
(1999)  Structure  7 : 1135 - 1143

DOI: 10.1016/S0969-2126(99)80180-4

Chain : B, D, F, H, J, L
UniProt : Q14790 (CASP8_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala). 3.4.22.61 PubMed:16916640, PubMed:23516580, PubMed:32929201, PubMed:34012073, PubMed:8962078
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