3er3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:3er3.jpg|left|200px]]
[[Image:3er3.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 3er3 |SIZE=350|CAPTION= <scene name='initialview01'>3er3</scene>, resolution 2.0&Aring;
+
The line below this paragraph, containing "STRUCTURE_3er3", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</scene>, <scene name='pdbligand=CAL:5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISOBUTYL-HEXANOIC+ACID'>CAL</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|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>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_3er3| PDB=3er3 | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3er3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3er3 OCA], [http://www.ebi.ac.uk/pdbsum/3er3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3er3 RCSB]</span>
+
-
}}
+
'''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''
'''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''
Line 19: Line 16:
==About this Structure==
==About this Structure==
-
3ER3 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=3ER3 OCA].
+
3ER3 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ER3 OCA].
==Reference==
==Reference==
Line 30: Line 27:
[[Category: Hoover, D.]]
[[Category: Hoover, D.]]
[[Category: Veerapandian, B.]]
[[Category: Veerapandian, B.]]
-
[[Category: hydrolase (acid proteinase)]]
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:00:49 2008''
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:33:06 2008''
+

Revision as of 19:00, 4 May 2008

Image:3er3.jpg

Template:STRUCTURE 3er3

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

3ER3 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 22:00:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3er3"
Personal tools