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Ligands
Code Name Style Show Link
FXN 5-fluoro-1h-indole-2-carboxylic acid-(2-mercapto-ethyl)-amide
Non-standard Residues
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Glycosylation
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Code : 1SHL   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : CASPASE-7 IN COMPLEX WITH FICA ALLOSTERIC INHIBITOR
Release Data : 2004-08-17
Compound :
mol_id molecule chains synonym
1 Caspase-7 A,B ICE-like apoptotic protease 3, ICE-LAP3, Apoptotic protease Mch-3, CMH-1
ec: 3.4.22.-
mutation: D192A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
gene: CASP7, MCH3
expression_system_strain: BL21 (DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pJH07, pJH08
other_details: Caspase-7 large and small subunits were co-expressed from two separate plasmids , yielding a large subunit of residues 57-199 and a small subunit of residues 21 0-303 with the addition of eight amino acids QLHHHHHH.
Authors : Hardy, J.A., Lam, J., Nguyen, J.T., O'Brien, T., Wells, J.A.
Keywords : caspase, protease, cysteine protease, allosteric, central-cavity, dimer interface, inhibitor, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 3.00 Å )
Citation :

Discovery of an allosteric site in the caspases

Hardy, J.A.,Lam, J.,Nguyen, J.T.  et al.
(2004)  Proc.Natl.Acad.Sci.USA  101 : 12461 - 12466

PubMed: 15314233
DOI: 10.1073/pnas.0404781101

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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