1F1J
CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO
Summary for 1F1J
Entry DOI | 10.2210/pdb1f1j/pdb |
Related PRD ID | PRD_000422 |
Descriptor | CASPASE-7 PROTEASE, ACE-ASP-GLU-VAL-ASP-CHO, SULFATE ION, ... (4 entities in total) |
Functional Keywords | caspase-7, cysteine protease, hydrolase, apoptosis, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm: P55210 |
Total number of polymer chains | 4 |
Total formula weight | 70269.17 |
Authors | Wei, Y.,Charifson, P.S. (deposition date: 2000-05-19, release date: 2001-05-23, Last modification date: 2013-07-03) |
Primary citation | Wei, 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: 10873833DOI: 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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