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1F1J

CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO

Summary for 1F1J
Entry DOI10.2210/pdb1f1j/pdb
Related PRD IDPRD_000422
DescriptorCASPASE-7 PROTEASE, ACE-ASP-GLU-VAL-ASP-CHO, SULFATE ION, ... (4 entities in total)
Functional Keywordscaspase-7, cysteine protease, hydrolase, apoptosis, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm: P55210
Total number of polymer chains4
Total formula weight70269.17
Authors
Wei, Y.,Charifson, P.S. (deposition date: 2000-05-19, release date: 2001-05-23, Last modification date: 2013-07-03)
Primary citationWei, Y.,Fox, T.,Chambers, S.P.,Sintchak, J.,Coll, J.T.,Golec, J.M.,Swenson, L.,Wilson, K.P.,Charifson, P.S.
The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity.
Chem.Biol., 7:423-432, 2000
Cited by
PubMed Abstract: Peptide inhibitors of caspases have helped define the role of these cysteine proteases in biology. Structural and biochemical characterization of the caspase enzymes may contribute to the development of new drugs for the treatment of caspase-mediated inflammation and apoptosis.
PubMed: 10873833
DOI: 10.1016/S1074-5521(00)00123-X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.35 Å)
Structure validation

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數據於2024-11-06公開中

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