1QCP

CRYSTAL STRUCTURE OF THE RWJ-51084 BOVINE PANCREATIC BETA-TRYPSIN AT 1.8 A

Summary for 1QCP

• Entry DOI: 10.2210/pdb1qcp/pdb
• Descriptor: PROTEIN (BETA-TRYPSIN PROTEIN), CALCIUM ION, CYCLOPENTANECARBOXYLIC ACID [1-(BENZOTHIAZOLE-2-CARBONYL)-4-GUANIDINO-BUTYL]-AMIDE, ... (4 entities in total)
• Functional Keywords: serine protease-inhibitor complex, hydrolase
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted, extracellular space: P00760
• Total number of polymer chains: 1
• Total formula weight: 23751.86

Authors

Recacha, R.,Carson, M.,Costanzo, M.J.,Maryanoff, B.,Chattopadhyay, D. (deposition date: 1999-05-10, release date: 1999-05-21, Last modification date: 2024-10-16)

Primary citation

Recacha, R.,Carson, M.,Costanzo, M.J.,Maryanoff, B.,DeLucas, L.J.,Chattopadhyay, D.
Structure of the RWJ-51084-bovine pancreatic beta-trypsin complex at 1.8 A.
Acta Crystallogr.,Sect.D, 55:1785-1791, 1999

PubMed Abstract: The three-dimensional structure of bovine pancreatic trypsin complexed with the inhibitor RWJ-51084 has been determined at 1.8 A resolution. These crystals belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 53.43, c = 107.76 A. The refined R and R(free) values are 0.175 and 0.237, respectively. The carbonyl group bonded to the benzothiazole group of the inhibitor is covalently linked to the hydroxyl O atom of Ser195, forming a tetrahedral intermediate hemiketal structure. The other carbonyl O atom of the inhibitor forms a hydrogen bond with the Gln192 side-chain amide group. The benzothiazole group is oriented with the aromatic N atom of RWJ-51084 accepting a hydrogen bond from His57 NE2. The arginine side chain of the inhibitor extends into the deep and narrow pocket of the S1 specificity site of trypsin, forming a network of hydrogen bonds.

PubMed: 10531473
DOI: 10.1107/S0907444999008732

Experimental method

X-RAY DIFFRACTION (1.8 Å)