5cha

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[[Image:5cha.png|left|200px]]
 
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==THE REFINEMENT AND THE STRUCTURE OF THE DIMER OF ALPHA-*CHYMOTRYPSIN AT 1.67-*ANGSTROMS RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_5cha", creates the "Structure Box" on the page.
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<StructureSection load='5cha' size='340' side='right'caption='[[5cha]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[5cha]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3cha 3cha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CHA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cha OCA], [https://pdbe.org/5cha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cha RCSB], [https://www.ebi.ac.uk/pdbsum/5cha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cha ProSAT]</span></td></tr>
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{{STRUCTURE_5cha| PDB=5cha | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/5cha_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=5cha ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The two molecules of the asymmetric unit of the pH 3.5 conformer of alpha-chymotrypsin have been refined at 1.67-A resolution using restrained least squares methods with Hendrickson's program (PROLSQ). The final R factor is 0.179 (including 247 water molecules). The folding of the main chain of the independent molecules is the same within experimental error but the same does not generally apply to the side chain stereochemistry. From this we conclude that the folding of a protein structure is basically independent of most of the detailed stereochemistry of its side chains. The side chains of the interface region between the independent molecules display pronounced asymmetry. This asymmetry suggests that dynamic and asymmetrical structural changes take place at the time of oligomerization leading to more energetically favorable interactions for the dimer. Comparison of the structures of the independent molecules of alpha-chymotrypsin with the structure of monomeric gamma-chymotrypsin revealed that although the folding of the three molecules is essentially the same, numerous and significant differences pervade the side chain stereochemistry attributable to general flexibility. The specificity site of alpha-chymotrypsin is occupied by ordered water molecules in a similar way to gamma-chymotrypsin and other proteins. Some of these water molecules are displaced when substrate binds to the enzyme, while the others appear to help identify and position the aromatic side chain in catalysis.
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===THE REFINEMENT AND THE STRUCTURE OF THE DIMER OF ALPHA-*CHYMOTRYPSIN AT 1.67-*ANGSTROMS RESOLUTION===
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The refinement and the structure of the dimer of alpha-chymotrypsin at 1.67-A resolution.,Blevins RA, Tulinsky A J Biol Chem. 1985 Apr 10;260(7):4264-75. PMID:3980476<ref>PMID:3980476</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_3980476}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 5cha" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 3980476 is the PubMed ID number.
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{{ABSTRACT_PUBMED_3980476}}
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==About this Structure==
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[[5cha]] is a 6 chain structure of [[Chymotrypsin]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3cha 3cha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHA OCA].
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==See Also==
==See Also==
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*[[Chymotrypsin]]
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*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
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*[[Streptomyces griseus proteinase B|Streptomyces griseus proteinase B]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:3980476</ref><references group="xtra"/>
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Chymotrypsin]]
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[[Category: Large Structures]]
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[[Category: Blevins, R A.]]
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[[Category: Blevins RA]]
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[[Category: Tulinsky, A.]]
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[[Category: Tulinsky A]]

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THE REFINEMENT AND THE STRUCTURE OF THE DIMER OF ALPHA-*CHYMOTRYPSIN AT 1.67-*ANGSTROMS RESOLUTION

PDB ID 5cha

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