4er2: Difference between revisions

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[[Image:4er2.~~jpg~~|left|200px]]

[[Image:4er2.png|left|200px]]

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~~'''~~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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==About this Structure==

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[[Category: Cooper, J B.]]

[[Category: Veerapandian, B.]]

''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 13:35:50 2008''

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-[[Image:4er2.jpg|left|200px]]
+{{Seed}}
+[[Image:4er2.png|left|200px]]
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 {{STRUCTURE_4er2|  PDB=4er2  |  SCENE=  }}
-'''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''
+===THE ACTIVE SITE OF ASPARTIC PROTEINASES===
-==Overview==
+<!--
-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.
+-->
+{{ABSTRACT_PUBMED_6381096}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Cooper, J B.]]
 [[Category: Veerapandian, B.]]
-''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 13:35:50 2008''