1P2Q
Structural consequences of accommodation of four non-cognate amino-acid residues in the S1 pocket of bovine trypsin and chymotrypsin
Summary for 1P2Q
Entry DOI | 10.2210/pdb1p2q/pdb |
Related | 1P2I 1P2J 1P2K 1P2M 1P2N 1P2O |
Descriptor | Chymotrypsinogen A, Pancreatic trypsin inhibitor, SULFATE ION, ... (5 entities in total) |
Functional Keywords | trypsin; chymotrypsin; serine proteinase; bovine pancreatic trypsin inhibitor; protein-protein interaction; non-cognate binding; s1 pocket; primary specificity; crystal structure, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Bos taurus (cattle) More |
Cellular location | Secreted, extracellular space: P00766 Secreted: P00974 |
Total number of polymer chains | 4 |
Total formula weight | 65632.04 |
Authors | Helland, R.,Czapinska, H.,Leiros, I.,Olufsen, M.,Otlewski, J.,Smalaas, A.O. (deposition date: 2003-04-15, release date: 2004-04-20, Last modification date: 2023-08-16) |
Primary citation | Helland, R.,Czapinska, H.,Leiros, I.,Olufsen, M.,Otlewski, J.,Smalaas, A.O. Structural consequences of accommodation of four non-cognate amino acid residues in the S1 pocket of bovine trypsin and chymotrypsin. J.Mol.Biol., 333:845-861, 2003 Cited by PubMed: 14568540DOI: 10.1016/j.jmb.2003.08.059 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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