1acb

CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1acb, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1acb is a 2 chain structure with sequence from Bos taurus and Hirudo medicinalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Chymotrypsin, with EC number 3.4.21.1 Resources: FirstGlance, OCA, RCSB, PDBsum 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 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chymotrypsin Eglin

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