PDBsum entry 1qcp

Hydrolase

PDB id: 1qcp

Contents

Protein chain

223 a.a. *

Ligands

RWJ

Metals

_CA

Waters ×207

* Residue conservation analysis

PDB id:

1qcp

Name:

Hydrolase

Title:

Crystal structure of the rwj-51084 bovine pancreatic beta-trypsin at 1.8 a

Structure:

Protein (beta-trypsin protein). Chain: a

Source:

Bos taurus. Cattle. Organism_taxid: 9913

Resolution:

1.80Å R-factor: 0.175 R-free: 0.237

Authors:

R.Recacha,M.Carson,M.J.Costanzo,B.Maryanoff,D.Chattopadhyay

Key ref:

R.Recacha et al. (1999). Structure of the RWJ-51084-bovine pancreatic beta-trypsin complex at 1.8 A. Acta Crystallogr D Biol Crystallogr, 55, 1785-1791. PubMed id: 10531473 DOI: 10.1107/S0907444999008732

Date:

10-May-99 Release date: 21-May-99

Protein chain

P00760  (TRY1_BOVIN) -  Serine protease 1 from Bos taurus

Seq: 246 a.a.

Struc: 223 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.21.4 - trypsin.
• Reaction: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

DOI no: 10.1107/S0907444999008732

Acta Crystallogr D Biol Crystallogr 55:1785-1791 (1999)

PubMed id: 10531473

Structure of the RWJ-51084-bovine pancreatic beta-trypsin complex at 1.8 A.

R.Recacha, M.Carson, M.J.Costanzo, B.Maryanoff, L.J.DeLucas, D.Chattopadhyay.

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.

Selected figure(s)

Figure 1.
Figure 1 Chemical formula of RWJ-51084.

Figure 2.
Figure 2 Ribbon plot of the complex formed between trypsin and RWJ-51084. Side chains of the catalytic triad residues His57, Asp102 and Ser195 are explicitly shown, as well as the calcium cation on the right. All figures prepared with Ribbons, [67]http://www.cmc.uab.edu/ribbons (Carson, 1997[68] [Carson, M. (1997). Methods Enzymol. 277, 493-505.]-[69][bluearr.gif] ).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 1785-1791) copyright 1999.

Figures were selected by an automated process.