2ahk: Difference between revisions

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 ==Crystal structure of the met-form of the copper-bound Streptomyces castaneoglobisporus tyrosinase in complex with a caddie protein obtained by soking in cupric sulfate for 6 months==
-<StructureSection load='2ahk' size='340' side='right' caption='[[2ahk]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
+<StructureSection load='2ahk' size='340' side='right'caption='[[2ahk]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ahk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_castaneoglobisporus Streptomyces castaneoglobisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AHK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ahk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_castaneoglobisporus Streptomyces castaneoglobisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AHK FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 1.71&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wx2|1wx2]], [[1wx3|1wx3]], [[1wx4|1wx4]], [[1wx5|1wx5]], [[1wxc|1wxc]], [[2ahl|2ahl]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TYRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79261 Streptomyces castaneoglobisporus]), ORF378 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79261 Streptomyces castaneoglobisporus])</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=2ahk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahk OCA], [https://pdbe.org/2ahk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ahk RCSB], [https://www.ebi.ac.uk/pdbsum/2ahk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahk ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monophenol_monooxygenase Monophenol monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.18.1 1.14.18.1] </span></td></tr>
+</table>
-<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=2ahk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ahk RCSB], [http://www.ebi.ac.uk/pdbsum/2ahk PDBsum]</span></td></tr>
+== Function ==
-<table>
+[https://www.uniprot.org/uniprot/Q83WS2_9ACTN Q83WS2_9ACTN]
 == 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/ah/2ahk_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/2ahk_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=2ahk ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2ahk" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Monophenol monooxygenase]]
+[[Category: Large Structures]]
 [[Category: Streptomyces castaneoglobisporus]]
-[[Category: Kumagai, T.]]
+[[Category: Kumagai T]]
-[[Category: Matoba, Y.]]
+[[Category: Matoba Y]]
-[[Category: Sugiyama, M.]]
+[[Category: Sugiyama M]]
-[[Category: Yamamoto, A.]]
+[[Category: Yamamoto A]]
-[[Category: Yoshitsu, H.]]
+[[Category: Yoshitsu H]]
-[[Category: Binary complex]]
-[[Category: Oxidoreductase-metal transport complex]]
-[[Category: Tyrosinase]]