4er2

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[[Image:4er2.jpg|left|200px]]
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{{STRUCTURE_4er2| PDB=4er2 | SCENE= }}
{{STRUCTURE_4er2| PDB=4er2 | SCENE= }}
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'''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''
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===THE ACTIVE SITE OF ASPARTIC PROTEINASES===
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==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.
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(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: Cooper, J B.]]
[[Category: Cooper, J B.]]
[[Category: Veerapandian, B.]]
[[Category: Veerapandian, B.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:23:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:35:50 2008''

Revision as of 10:35, 3 July 2008

Image:4er2.png

Template:STRUCTURE 4er2

THE ACTIVE SITE OF ASPARTIC PROTEINASES

Template:ABSTRACT PUBMED 6381096

About this Structure

4ER2 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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