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New page: left|200px<br /><applet load="4cha" size="450" color="white" frame="true" align="right" spinBox="true" caption="4cha, resolution 1.68Å" /> '''STRUCTURE OF ALPHA-*...
 
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[[Image:4cha.gif|left|200px]]<br /><applet load="4cha" size="450" color="white" frame="true" align="right" spinBox="true"
caption="4cha, resolution 1.68&Aring;" />
'''STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION'''<br />


==Overview==
==STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION==
Diffraction data for alpha-chymotrypsin crystals at -10 degrees C were, measured at 1.68 A resolution and refined by restrained structure-factor, least-squares refinement. The two independent chymotrypsin molecules in, the crystallographic asymmetric unit were refined independently. The, overall structure of alpha-chymotrypsin is little changed from published, co-ordinates. The root-mean-square shift of C alpha co-ordinates is 0.42, A, co-ordinates for the two molecules showing a root-mean-square, difference of 0.19 A. Certain regions with high disorder (residues 9 to, 14, 73 to 79) remain difficult to interpret and several side-chains are, disordered. Some water molecule positions have been changed. The absence, of the tosyl group has made a significant difference to the refined, structure at the active site. This now agrees closely with other enzymes, of the trypsin family that have been refined at high resolution. There is, a strong hydrogen bond between N epsilon 2 (His57) and O gamma (Ser195) in, the free enzyme, in line with the published description of the charge, relay system.
<StructureSection load='4cha' size='340' side='right'caption='[[4cha]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cha]] is a 6 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=4CHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cha OCA], [https://pdbe.org/4cha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cha RCSB], [https://www.ebi.ac.uk/pdbsum/4cha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cha 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/ch/4cha_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=4cha ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Diffraction data for alpha-chymotrypsin crystals at -10 degrees C were measured at 1.68 A resolution and refined by restrained structure-factor least-squares refinement. The two independent chymotrypsin molecules in the crystallographic asymmetric unit were refined independently. The overall structure of alpha-chymotrypsin is little changed from published co-ordinates. The root-mean-square shift of C alpha co-ordinates is 0.42 A, co-ordinates for the two molecules showing a root-mean-square difference of 0.19 A. Certain regions with high disorder (residues 9 to 14, 73 to 79) remain difficult to interpret and several side-chains are disordered. Some water molecule positions have been changed. The absence of the tosyl group has made a significant difference to the refined structure at the active site. This now agrees closely with other enzymes of the trypsin family that have been refined at high resolution. There is a strong hydrogen bond between N epsilon 2 (His57) and O gamma (Ser195) in the free enzyme, in line with the published description of the charge relay system.


==About this Structure==
Structure of alpha-chymotrypsin refined at 1.68 A resolution.,Tsukada H, Blow DM J Mol Biol. 1985 Aug 20;184(4):703-11. PMID:4046030<ref>PMID:4046030</ref>
4CHA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4CHA OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of alpha-chymotrypsin refined at 1.68 A resolution., Tsukada H, Blow DM, J Mol Biol. 1985 Aug 20;184(4):703-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=4046030 4046030]
</div>
<div class="pdbe-citations 4cha" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Chymotrypsin]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Blow DM]]
[[Category: Blow, D.M.]]
[[Category: Tsukada H]]
[[Category: Tsukada, H.]]
[[Category: hydrolase (serine proteinase)]]
 
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Latest revision as of 08:23, 23 October 2024

STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION

4cha, resolution 1.68Å

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