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Ligands
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0TE Chloro{methyl hydrogenato(3-)-kappa~2~N,S [pyridin-2-yl(pyridin-2(1h)-ylidene-kappan)methyl]carbonodithiohydrazonate}copper
Non-standard Residues
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Code : 4FEA   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystal structure of CASPASE-7 in Complex with allosteric inhibitor
Release Data : 2012-08-01
Compound :
mol_id molecule chains synonym
1 Caspase-7 A,B CASP-7, Apoptotic protease Mch-3, CMH-1, ICE-like apoptotic protease 3, ICE-LAP3
ec: 3.4.22.60
fragment: P20/P10 catalytic domain (UNP residues 57-303)
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: CASP7, MCH3
Authors : Kabaleeswaran, V.
Keywords : cysteine protease, apoptosis, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 3.7900 Å )
Citation :

A class of allosteric caspase inhibitors identified by high-throughput screening.

Feldman, T.,Kabaleeswaran, V.,Jang, S.B.  et al.
(2012)  Mol.Cell  47 : 585 - 595

PubMed: 22795132
DOI: 10.1016/j.molcel.2012.06.007

Chain : A, B
UniProt : P55210 (CASP7_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-. 3.4.22.60 PubMed:10497198, PubMed:11257230, PubMed:11701129, PubMed:12824163, PubMed:16123041, PubMed:16374543, PubMed:16916640, PubMed:17646170, PubMed:17697120, PubMed:18723680, PubMed:19581639, PubMed:19617626, PubMed:20566630, PubMed:22451931, PubMed:23650375, PubMed:23897474, PubMed:27032039, PubMed:31586028, PubMed:34156061
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