4er1: Difference between revisions

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[[Image:4er1.jpg|left|200px]]
{{Seed}}
[[Image:4er1.png|left|200px]]


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{{STRUCTURE_4er1|  PDB=4er1  |  SCENE=  }}  
{{STRUCTURE_4er1|  PDB=4er1  |  SCENE=  }}  


'''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''
===THE ACTIVE SITE OF ASPARTIC PROTEINASES===




==Overview==
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The active site of the aspartic proteinase, endothiapepsin, has been defined by X-ray analysis and restrained least-squares refinement at 2.1 A resolution with a crystallographic agreement value of 0.16. The environments of the two catalytically important aspartyl groups are remarkably similar and the contributions of the NH2- and COOH-terminal domains to the catalytic centre are related by a local 2-fold axis. The carboxylates of the aspartyls share a hydrogen bond and have equivalent contacts to a bound water molecule or hydroxonium ion lying on the local diad. The main chains around 32 and 215 are connected by a novel interaction involving diad-related threonines. It is suggested that the two pKa values of the active site aspartyls arise from a structure not unlike that in maleic acid with a hydrogen-bonded intermediate species and a dicarboxylate characterised by electrostatic repulsions between the two negatively charged groups.
The line below this paragraph, {{ABSTRACT_PUBMED_6381096}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 6381096 is the PubMed ID number.
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{{ABSTRACT_PUBMED_6381096}}


==About this Structure==
==About this Structure==
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[[Category: Quail, J W.]]
[[Category: Quail, J W.]]
[[Category: Szelke, M.]]
[[Category: Szelke, M.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:23:30 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:35:44 2008''

Revision as of 10:35, 3 July 2008

File:4er1.png

Template:STRUCTURE 4er1

THE ACTIVE SITE OF ASPARTIC PROTEINASES

Template:ABSTRACT PUBMED 6381096

About this Structure

4ER1 is a Single protein structure. Full crystallographic information is available from OCA.

Reference

The active site of aspartic proteinases., Pearl L, Blundell T, FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:6381096

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