1acb
From Proteopedia
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CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION
Overview
The crystal structure of the complex between bovine alpha-chymotrypsin and, the leech (Hirudo medicinalis) protein proteinase inhibitor eglin c has, been refined at 2.0 A resolution to a crystallographic R-factor of 0.167., The structure of the complex includes 2290 protein and 143 solvent atoms., Eglin c is bound to the cognate enzyme through interactions involving 11, residues of the inhibitor (sites P5-P4' in the reactive site loop, P10', and P23') and 17 residues from chymotrypsin. Binding of eglin c to the, enzyme causes a contained hinge-bending movement around residues P4 and, P4' of the inhibitor. The tertiary structure of chymotrypsin is little, affected, with the exception of the 10-13 region, where an ordered, structure for the polypeptide chain is observed. The overall binding mode, is consistent with those found in other serine, proteinase-protein-inhibitor complexes, including those from different, inhibition families. Contained, but significant differences are observed, in the establishment of intramolecular hydrogen bonds and polar, interactions stabilizing the structure of the intact inhibitor, if the, structure of eglin c in its complex with chymotrypsin is compared with, that of other eglin c-serine proteinase complexes.
About this Structure
1ACB is a Protein complex structure of sequences from [1]. Active as Chymotrypsin, with EC number 3.4.21.1 Full crystallographic information is available from OCA.
Reference
Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution., Frigerio F, Coda A, Pugliese L, Lionetti C, Menegatti E, Amiconi G, Schnebli HP, Ascenzi P, Bolognesi M, J Mol Biol. 1992 May 5;225(1):107-23. PMID:1583684
Page seeded by OCA on Tue Nov 20 10:45:10 2007
