2agg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:24, 23 August 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2agg.png|left|200px]]
 
-
<!--
+
==succinyl-AAPK-trypsin acyl-enzyme at 1.28 A resolution==
-
The line below this paragraph, containing "STRUCTURE_2agg", creates the "Structure Box" on the page.
+
<StructureSection load='2agg' size='340' side='right'caption='[[2agg]], [[Resolution|resolution]] 1.28&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2agg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AGG FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.28&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
{{STRUCTURE_2agg| PDB=2agg | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2agg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2agg OCA], [https://pdbe.org/2agg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2agg RCSB], [https://www.ebi.ac.uk/pdbsum/2agg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2agg ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/2agg_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2agg ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of this classic serine protease. Structural comparisons provide insight into active site adjustments involved in catalysis. Subtle motions of the catalytic serine and histidine residues coordinated with translation of the substrate reaction center are seen to favor the forward progress of the acylation reaction. The structures also clarify the attack trajectory of the hydrolytic water in the deacylation reaction.
-
===succinyl-AAPK-trypsin acyl-enzyme at 1.28 A resolution===
+
Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates.,Radisky ES, Lee JM, Lu CJ, Koshland DE Jr Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277<ref>PMID:16636277</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2agg" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_16636277}}, adds the Publication Abstract to the page
+
*[[Proteins from Mycobacterium tuberculosis|Proteins from Mycobacterium tuberculosis]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 16636277 is the PubMed ID number.
+
*[[Trypsin 3D structures|Trypsin 3D structures]]
-
-->
+
== References ==
-
{{ABSTRACT_PUBMED_16636277}}
+
<references/>
-
 
+
__TOC__
-
==About this Structure==
+
</StructureSection>
-
2AGG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGG OCA].
+
-
 
+
-
==Reference==
+
-
Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates., Radisky ES, Lee JM, Lu CJ, Koshland DE Jr, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16636277 16636277]
+
[[Category: Bos taurus]]
[[Category: Bos taurus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Trypsin]]
+
[[Category: Koshland Jr DE]]
-
[[Category: Jr., D E.Koshland.]]
+
[[Category: Lee JM]]
-
[[Category: Lee, J M.]]
+
[[Category: Lu CJ]]
-
[[Category: Lu, C J.]]
+
[[Category: Radisky ES]]
-
[[Category: Radisky, E S.]]
+
-
[[Category: Acyl-enzyme]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Peptidase]]
+
-
[[Category: Proteinase]]
+
-
[[Category: Serine protease]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:05:01 2008''
+

Current revision

succinyl-AAPK-trypsin acyl-enzyme at 1.28 A resolution

PDB ID 2agg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2agg"
Personal tools