1szo: Difference between revisions

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 ==Crystal Structure Analysis of the 6-Oxo Camphor Hydrolase His122Ala Mutant Bound to Its Natural Product (2S,4S)-alpha-Campholinic Acid==
-<StructureSection load='1szo' size='340' side='right' caption='[[1szo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='1szo' size='340' side='right'caption='[[1szo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1szo]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_sp._ncimb_9784 Rhodococcus sp. ncimb 9784]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SZO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SZO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1szo]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_sp._NCIMB_9784 Rhodococcus sp. NCIMB 9784]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SZO FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CAX:(2S,4S)-4-(2,2-DIHYDROXYETHYL)-2,3,3-TRIMETHYLCYCLOPENTANONE'>CAX</scene><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]] 1.9&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1o8u|1o8u]], [[1dub|1dub]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CAX:(2S,4S)-4-(2,2-DIHYDROXYETHYL)-2,3,3-TRIMETHYLCYCLOPENTANONE'>CAX</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">camK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=157732 Rhodococcus sp. NCIMB 9784])</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=1szo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1szo OCA], [https://pdbe.org/1szo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1szo RCSB], [https://www.ebi.ac.uk/pdbsum/1szo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1szo ProSAT]</span></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=1szo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1szo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1szo RCSB], [http://www.ebi.ac.uk/pdbsum/1szo PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[https://www.uniprot.org/uniprot/CAMK_RHOSO CAMK_RHOSO] Catalyzes the carbon-carbon bond cleavage of the bicyclic beta-diketone 6-oxocamphor via a retro-Claisen reaction to yield the optically active (2R,4S)-beta-campholinic acid. It is also able to cleave 2,2-disubstituted cyclohexa-1,3-diones such as 2-methyl-2-propylcyclohexa-1,3-dione and 2-methyl-2-butylcyclohexa-1,3-dione which result in racemic keto acid products. Transformations of the bicyclic diketone substrates bicyclo[2.2.1]heptane 2,6-dione and bicyclo[2.2.2]octane-2,6-dione yield (S)-keto acid products.<ref>PMID:11278926</ref> <ref>PMID:15138275</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/sz/1szo_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sz/1szo_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=1szo ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
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 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1szo" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Rhodococcus sp. ncimb 9784]]
+[[Category: Large Structures]]
-[[Category: Grogan, G.]]
+[[Category: Rhodococcus sp. NCIMB 9784]]
-[[Category: Leonard, P M.]]
+[[Category: Grogan G]]
-[[Category: Enzyme-product complex]]
+[[Category: Leonard PM]]
-[[Category: Hydrolase]]