1suc: Difference between revisions

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-[[Image:1suc.png|left|200px]]
-<!--
+==CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN==
-The line below this paragraph, containing "STRUCTURE_1suc", creates the "Structure Box" on the page.
+<StructureSection load='1suc' size='340' side='right'caption='[[1suc]], [[Resolution|resolution]] 1.80&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'>[[1suc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUC 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]] 1.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
-{{STRUCTURE_1suc|  PDB=1suc  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1suc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suc OCA], [https://pdbe.org/1suc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1suc RCSB], [https://www.ebi.ac.uk/pdbsum/1suc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1suc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SUBT_BACAM SUBT_BACAM] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.<ref>PMID:12524032</ref>
+== 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/su/1suc_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=1suc ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A version of subtilisin BPN' lacking the high affinity calcium site (site A) has been produced through genetic engineering methods, and its crystal structure refined at 1.8 A resolution. This protein and the corresponding version containing the calcium A site are described and compared. The deletion of residues 75-83 was made in the context of four site-specific replacements previously shown to stabilize subtilisin. The helix that in wild type is interrupted by the calcium binding loop, is continuous in the deletion mutant, with normal geometry. A few residues adjacent to the loop, principally those that were involved in calcium coordination, are repositioned and/or destabilized by the deletion. Because refolding is greatly facilitated by the absence of the Ca-loop, this protein offers a new vehicle for analysis and dissection of the folding reaction. This is among the largest internal changes to a protein to be described at atomic resolution.
-===CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN===
+Calcium-independent subtilisin by design.,Gallagher T, Bryan P, Gilliland GL Proteins. 1993 Jun;16(2):205-13. PMID:8332608<ref>PMID:8332608</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_8332608}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1suc" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 8332608 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_8332608}}
-==About this Structure==
-[[1suc]] is a 1 chain structure of [[Subtilisin]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUC OCA].
 ==See Also==
-*[[Subtilisin]]
+*[[Subtilisin 3D structures|Subtilisin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:8332608</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Bacillus amyloliquefaciens]]
-[[Category: Subtilisin]]
+[[Category: Large Structures]]
-[[Category: Bryan, P.]]
+[[Category: Bryan P]]
-[[Category: Gallagher, T.]]
+[[Category: Gallagher T]]
-[[Category: Gilliland, G L.]]
+[[Category: Gilliland GL]]