1LW6

Crystal Structure of the Complex of Subtilisin BPN' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution

Summary for 1LW6

Entry DOI	10.2210/pdb1lw6/pdb
Descriptor	SUBTILISIN BPN', SUBTILISIN-CHYMOTRYPSIN INHIBITOR-2A, CALCIUM ION, ... (5 entities in total)
Functional Keywords	serine protease, inhibitor, hydrolase
Biological source	Bacillus amyloliquefaciens More
Total number of polymer chains	2
Total formula weight	36061.31
Authors	Radisky, E.S.,Koshland JR., D.E. (deposition date: 2002-05-30, release date: 2002-08-21, Last modification date: 2024-02-14)
Primary citation	Radisky, E.S.,Koshland Jr., D.E. A clogged gutter mechanism for protease inhibitors. Proc.Natl.Acad.Sci.USA, 99:10316-10321, 2002 Cited by PubMed Abstract: A classical peptide inhibitor of serine proteases that is hydrolyzed approximately 10(7) times more slowly than a good substrate is shown to form an acyl-enzyme intermediate rapidly. Despite this quick first step, further reaction is slowed dramatically because of tight and oriented binding of the cleaved peptide, preventing acyl-enzyme hydrolysis and favoring the reverse reaction. Moreover, this mechanism appears to be common to a large class of tight-binding serine protease inhibitors that mimic good substrates. The arrest of enzymatic reaction at the intermediate stage allowed us to determine that the consensus nucleophilic attack angle is close to 90 degrees in the reactive Michaelis complexes. PubMed: 12142461 DOI: 10.1073/pnas.112332899 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation