4caa: Difference between revisions

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 ==CLEAVED ANTICHYMOTRYPSIN T345R==
-<StructureSection load='4caa' size='340' side='right' caption='[[4caa]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='4caa' size='340' side='right'caption='[[4caa]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4caa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ct3 1ct3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CAA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CAA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4caa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ct3 1ct3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CAA FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4caa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4caa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4caa RCSB], [http://www.ebi.ac.uk/pdbsum/4caa PDBsum]</span></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=4caa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4caa OCA], [https://pdbe.org/4caa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4caa RCSB], [https://www.ebi.ac.uk/pdbsum/4caa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4caa ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AACT_HUMAN AACT_HUMAN] Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2.<ref>PMID:2404007</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/ca/4caa_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ca/4caa_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=4caa ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 22: / Line 25: @@
 Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction.,Lukacs CM, Rubin H, Christianson DW Biochemistry. 1998 Mar 10;37(10):3297-304. PMID:9521649<ref>PMID:9521649</ref>
-From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4caa" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Serpin 3D structures|Serpin 3D structures]]
 == References ==
 <references/>
@@ Line 29: / Line 36: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Christianson, D W.]]
+[[Category: Large Structures]]
-[[Category: Lukacs, C M.]]
+[[Category: Christianson DW]]
-[[Category: Antichymotrypsin]]
+[[Category: Lukacs CM]]
-[[Category: Serine protease inhibitor]]
-[[Category: Serpin]]