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2zwe
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zwe]] 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=2ZWE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZWE FirstGlance]. <br> | <table><tr><td colspan='2'>[[2zwe]] 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=2ZWE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZWE 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>< | + | </td></tr><tr id='ligand'><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></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wxc|1wxc]], [[1wx2|1wx2]], [[2zmx|2zmx]], [[2zmy|2zmy]], [[2zmz|2zmz]], [[2zwc|2zwc]], [[2zwd|2zwd]], [[2zwf|2zwf]], [[2zwg|2zwg]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wxc|1wxc]], [[1wx2|1wx2]], [[2zmx|2zmx]], [[2zmy|2zmy]], [[2zmz|2zmz]], [[2zwc|2zwc]], [[2zwd|2zwd]], [[2zwf|2zwf]], [[2zwg|2zwg]]</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='gene'><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><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> | + | <tr id='activity'><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> |
| - | <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=2zwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zwe RCSB], [http://www.ebi.ac.uk/pdbsum/2zwe PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zwe RCSB], [http://www.ebi.ac.uk/pdbsum/2zwe PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis.,Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M J Biol Chem. 2006 Mar 31;281(13):8981-90. Epub 2006 Jan 25. PMID:16436386<ref>PMID:16436386</ref> | Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis.,Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M J Biol Chem. 2006 Mar 31;281(13):8981-90. Epub 2006 Jan 25. PMID:16436386<ref>PMID:16436386</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
Revision as of 06:43, 10 October 2014
Crystal structure of the copper-bound tyrosinase in complex with a caddie protein from streptomyces castaneoglobisporus obtained by soaking the deoxy-form crystal in dioxygen-saturated solution for 40 minutes
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