1czi
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(New page: 200px<br /> <applet load="1czi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1czi, resolution 2.30Å" /> '''CHYMOSIN COMPLEX WI...)
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Revision as of 18:07, 29 October 2007
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CHYMOSIN COMPLEX WITH THE INHIBITOR CP-113972
Overview
In the crystal structure of uncomplexed native chymosin, the beta-hairpin, at the active site, known as 'the flap', adopts a different conformation, from that of other aspartic proteinases. This conformation would prevent, the mode of binding of substrates/inhibitors generally found in other, aspartic proteinase complexes. We now report the X-ray analysis of, chymosin complexed with a reduced bond inhibitor CP-113972 inverted, question mark(2R,3S)-isopropyl, 3-[(L-prolyl-p-iodo-L-phenylalanyl-S-methyl-cysteinyl)amino-4]-cyclohexy, l-2-hydroxybutanoate inverted question mark at 2.3 A resolution in a novel, crystal form of spacegroup R32. The structure has been refined by, restrained least-squares methods to a final R-factor of 0.19 for a total, of 11 988 independent reflections in the ... [(full description)]
About this Structure
1CZI is a [Single protein] structure of sequence from [Bos taurus]. Active as [[1]], with EC number [3.4.23.4]. Full crystallographic information is available from [OCA].
Reference
A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure., Groves MR, Dhanaraj V, Badasso M, Nugent P, Pitts JE, Hoover DJ, Blundell TL, Protein Eng. 1998 Oct;11(10):833-40. PMID:9862200
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