3gch: Difference between revisions

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{{Seed}}
[[Image:3gch.png|left|200px]]


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==CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN==
The line below this paragraph, containing "STRUCTURE_3gch", creates the "Structure Box" on the page.
<StructureSection load='3gch' size='340' side='right'caption='[[3gch]], [[Resolution|resolution]] 1.90&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'>[[3gch]] is a 3 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=3GCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GCH 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]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OAC:TRANS-O-HYDROXY-ALPHA-METHYL+CINNAMATE'>OAC</scene></td></tr>
{{STRUCTURE_3gch|  PDB=3gch  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gch OCA], [https://pdbe.org/3gch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gch RCSB], [https://www.ebi.ac.uk/pdbsum/3gch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gch ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_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/gc/3gch_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3gch ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The serine protease gamma-chymotrypsin was covalently inhibited with two different photoreversible cinnamate compounds, and the structures of the resulting complexes were determined to 1.9-A resolution. The inhibitors show different kinetics of binding, inhibition, and nonphotochemical deacylation relative to each other in solution activity assays. The crystal structures of the enzyme-cinnamate complexes show that both compounds acylate serine 195 and that the two molecules are bound in similar nonproductive conformations which have drastic effects on their ability to turn over. Substitution of a diethylamino group on the para position of the cinnamate ring causes a 1000-fold increase in the thermal stability of the inhibitor toward hydrolysis and deacylation.


===CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN===
Structure and activity of two photoreversible cinnamates bound to chymotrypsin.,Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA Biochemistry. 1990 May 22;29(20):4871-9. PMID:2364065<ref>PMID:2364065</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3gch" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_2364065}}, adds the Publication Abstract to the page
*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 2364065 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_2364065}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Bos taurus]]
3GCH is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GCH OCA].
[[Category: Large Structures]]
 
[[Category: Petsko GA]]
==Reference==
[[Category: Ringe D]]
Structure and activity of two photoreversible cinnamates bound to chymotrypsin., Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 May 22;29(20):4871-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2364065 2364065]
[[Category: Stoddard BL]]
 
Photolysis and deacylation of inhibited chymotrypsin., Stoddard BL, Bruhnke J, Koenigs P, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 Sep 4;29(35):8042-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2261462 2261462]
 
Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors., Brady K, Wei AZ, Ringe D, Abeles RH, Biochemistry. 1990 Aug 21;29(33):7600-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2271520 2271520]
 
Inhibition of chymotrypsin by peptidyl trifluoromethyl ketones: determinants of slow-binding kinetics., Brady K, Abeles RH, Biochemistry. 1990 Aug 21;29(33):7608-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2271521 2271521]
[[Category: Chymotrypsin]]
[[Category: Single protein]]
[[Category: Petsko, G A.]]
[[Category: Ringe, D.]]
[[Category: Stoddard, B L.]]
 
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Retrieved from "https://proteopedia.org/3gch"