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1gct

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IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?

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Retrieved from "http://52.214.119.220/wiki/index.php/1gct"

Categories: Bos taurus | Large Structures | Dixon MM | Matthews BW

@@ Line 1: / Line 1: @@
-[[Image:1gct.gif|left|200px]]
- {{Structure
+==IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?==
-|PDB= 1gct |SIZE=350|CAPTION= <scene name='initialview01'>1gct</scene>, resolution 1.6&Aring;
+<StructureSection load='1gct' size='340' side='right'caption='[[1gct]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
+<table><tr><td colspan='2'>[[1gct]] is a 4 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=1GCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GCT FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gct OCA], [https://pdbe.org/1gct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gct RCSB], [https://www.ebi.ac.uk/pdbsum/1gct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gct ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gct OCA], [http://www.ebi.ac.uk/pdbsum/1gct PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gct RCSB]</span>
+== 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/1gct_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=1gct ConSurf].
+<div style="clear:both"></div>
-'''IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?'''
+==See Also==
+*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., &amp; Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new refinement suggests that gamma-chymotrypsin, which is operationally defined by its crystalline habit, may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct.
+[[Category: Bos taurus]]
+[[Category: Large Structures]]
-==About this Structure==
+[[Category: Dixon MM]]
-GCT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCT OCA].
+[[Category: Matthews BW]]
-==Reference==
-Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?, Dixon MM, Matthews BW, Biochemistry. 1989 Aug 22;28(17):7033-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2819046 2819046]
-[[Category: Chymotrypsin]]
-[[Category: Protein complex]]
-[[Category: Dixon, M M.]]
-[[Category: Matthews, B W.]]
-[[Category: hydrolase (serine proteinase)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:31 2008''

1gct

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IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?

Structural highlights

Function

Evolutionary Conservation

See Also

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