1TPS

ATOMIC STRUCTURE OF THE TRYPSIN-A90720A COMPLEX: A UNIFIED APPROACH TO STRUCTURE AND FUNCTION

Summary for 1TPS

• Entry DOI: 10.2210/pdb1tps/pdb
• Descriptor: TRYPSIN, INHIBITOR A90720A, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Bos taurus (cattle); More
• Cellular location: Secreted, extracellular space: P00760
• Total number of polymer chains: 2
• Total formula weight: 24440.56

Authors

Lee, A.Y.,Clardy, J. (deposition date: 1994-09-04, release date: 1995-01-26, Last modification date: 2024-06-05)

Primary citation

Lee, A.Y.,Smitka, T.A.,Bonjouklian, R.,Clardy, J.
Atomic structure of the trypsin-A90720A complex: a unified approach to structure and function.
Chem.Biol., 1:113-117, 1994

PubMed Abstract: A90720A is a potent serine proteinase inhibitor produced by the terrestrial blue-green alga Microchaete loktakensis. Most of its structure has been defined by spectroscopic and degradative studies, but the configurations of several stereochemical centers are unknown, and its mode of inhibition of serine proteinases is not understood. We therefore examined the structure of the compound in a complex with trypsin.

PubMed: 9383379
DOI: 10.1016/1074-5521(94)90049-3

Experimental method

X-RAY DIFFRACTION (1.9 Å)