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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 DOI10.2210/pdb1p2q/pdb
Related1P2I 1P2J 1P2K 1P2M 1P2N 1P2O
DescriptorChymotrypsinogen A, Pancreatic trypsin inhibitor, SULFATE ION, ... (5 entities in total)
Functional Keywordstrypsin; 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 sourceBos taurus (cattle)
More
Cellular locationSecreted, extracellular space: P00766
Secreted: P00974
Total number of polymer chains4
Total formula weight65632.04
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 citationHelland, 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: 14568540
DOI: 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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