1czi: Difference between revisions
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'''CHYMOSIN COMPLEX WITH THE INHIBITOR CP-113972''' | {{Structure | ||
|PDB= 1czi |SIZE=350|CAPTION= <scene name='initialview01'>1czi</scene>, resolution 2.30Å | |||
|SITE= <scene name='pdbsite=AC1:Active+Site'>AC1</scene> and <scene name='pdbsite=AC2:Active+Site'>AC2</scene> | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Chymosin Chymosin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.4 3.4.23.4] | |||
|GENE= | |||
}} | |||
'''CHYMOSIN COMPLEX WITH THE INHIBITOR CP-113972''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CZI is a [ | 1CZI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZI OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9862200 9862200] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Chymosin]] | [[Category: Chymosin]] | ||
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[[Category: inhibitor complex]] | [[Category: inhibitor complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:30:51 2008'' | ||
Revision as of 11:30, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Sites: | and | ||||||
| Activity: | Chymosin, with EC number 3.4.23.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHYMOSIN COMPLEX WITH THE INHIBITOR CP-113972
OverviewOverview
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 resolution range 10 to 2.3 A. The extended beta-strand conformation of the inhibitor allows hydrogen bonds within the active site, while its sidechains make both electrostatic and hydrophobic interactions with residues lining the specificity pockets S4-->S1. The flap closes over the active site cleft in a way that closely resembles that of other previously determined aspartic proteinase inhibitor complexes. We conclude that the usual position and conformation of the flap found in other aspartic proteinases is available to native chymosin. The conformation observed in the native crystal form may result from intermolecular interactions between symmetry-related molecules in the crystal lattice.
About this StructureAbout this Structure
1CZI is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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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