3GJQ
Caspase-3 Binds Diverse P4 Residues in Peptides
Summary for 3GJQ
Entry DOI | 10.2210/pdb3gjq/pdb |
Related | 3GJR 3GJS 3GJT |
Descriptor | Caspase-3 subunit p17, Caspase-3 subunit p12, peptide inhibitor, ... (4 entities in total) |
Functional Keywords | enzyme catalysis, cysteine protease, protein recognition, apoptosis, cytoplasm, hydrolase, phosphoprotein, polymorphism, protease, s-nitrosylation, thiol protease, zymogen |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm: P42574 P42574 |
Total number of polymer chains | 6 |
Total formula weight | 59984.00 |
Authors | Fang, B.,Fu, G.,Agniswamy, J.,Harrison, R.W.,Weber, I.T. (deposition date: 2009-03-09, release date: 2009-03-24, Last modification date: 2011-07-13) |
Primary citation | Fang, B.,Fu, G.,Agniswamy, J.,Harrison, R.W.,Weber, I.T. Caspase-3 binds diverse P4 residues in peptides as revealed by crystallography and structural modeling. Apoptosis, 14:741-752, 2009 Cited by PubMed: 19283487DOI: 10.1007/s10495-009-0333-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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