Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of the RWJ-51084-bovine pancreatic beta-trypsin complex at 1.8 A.,Recacha R, Carson M, Costanzo MJ, Maryanoff B, DeLucas LJ, Chattopadhyay D Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1785-91. PMID:10531473[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Recacha R, Carson M, Costanzo MJ, Maryanoff B, DeLucas LJ, Chattopadhyay D. Structure of the RWJ-51084-bovine pancreatic beta-trypsin complex at 1.8 A. Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1785-91. PMID:10531473
