4er2

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[[Image:4er2.jpg|left|200px]]
[[Image:4er2.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 4er2 |SIZE=350|CAPTION= <scene name='initialview01'>4er2</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_4er2", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=STA:STATINE'>STA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_4er2| PDB=4er2 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4er2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4er2 OCA], [http://www.ebi.ac.uk/pdbsum/4er2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4er2 RCSB]</span>
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}}
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'''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''
'''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''
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==About this Structure==
==About this Structure==
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4ER2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ER2 OCA].
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4ER2 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ER2 OCA].
==Reference==
==Reference==
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[[Category: Cooper, J B.]]
[[Category: Cooper, J B.]]
[[Category: Veerapandian, B.]]
[[Category: Veerapandian, B.]]
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[[Category: hydrolase (acid proteinase)]]
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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 Mon Mar 31 05:38:36 2008''
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Revision as of 19:23, 4 May 2008

Image:4er2.jpg

Template:STRUCTURE 4er2

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.

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 Page seeded by OCA on Sun May 4 22:23:30 2008

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OCA

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