1cbx
From Proteopedia
|
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND THE BIPRODUCT ANALOG INHIBITOR L-BENZYLSUCCINATE AT 2.0 ANGSTROMS RESOLUTION
Overview
The X-ray crystal structure of the carboxypeptidase A-L-benzylsuccinate, complex has been refined at 2.0 A resolution to a final R-factor of 0.166., One molecule of the inhibitor binds to the enzyme active site. The, terminal carboxylate forms a salt link with the guanidinium group of, Arg145 and hydrogen bonds with Tyr248 and Asn144. The second carboxylate, group binds to the zinc ion in an asymmetric bidentate fashion replacing, the water molecule of the native structure. The zinc ion moves 0.5 A from, its position in the native structure to accommodate the inhibitor binding., The overall stereochemistry around the zinc can be considered a distorted, tetrahedron, although six atoms of the co-ordinated groups lie within 3.0, A from the zinc ion. The key for the strong inhibitory properties of, L-benzylsuccinate can be found in its ability both to co-ordinate the zinc, and to form a short carboxyl-carboxylate-type hydrogen bond (2.5 A) with, Glu270.
About this Structure
1CBX is a Single protein structure of sequence from Bos taurus with ZN and BZS as ligands. Active as Carboxypeptidase A, with EC number 3.4.17.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of the complex between carboxypeptidase A and the biproduct analog inhibitor L-benzylsuccinate at 2.0 A resolution., Mangani S, Carloni P, Orioli P, J Mol Biol. 1992 Jan 20;223(2):573-8. PMID:1738164
Page seeded by OCA on Tue Nov 20 12:19:49 2007
