2y9x: Difference between revisions
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<StructureSection load='2y9x' size='340' side='right'caption='[[2y9x]], [[Resolution|resolution]] 2.78Å' scene=''> | <StructureSection load='2y9x' size='340' side='right'caption='[[2y9x]], [[Resolution|resolution]] 2.78Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2y9x]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2y9x]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Agaricus_bisporus Agaricus bisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y9X FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0TR:2-HYDROXYCYCLOHEPTA-2,4,6-TRIEN-1-ONE'>0TR</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HO:HOLMIUM+ATOM'>HO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0TR:2-HYDROXYCYCLOHEPTA-2,4,6-TRIEN-1-ONE'>0TR</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HO:HOLMIUM+ATOM'>HO</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y9w|2y9w]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2y9w|2y9w]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tyrosinase Tyrosinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.18.1 1.14.18.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y9x OCA], [https://pdbe.org/2y9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y9x RCSB], [https://www.ebi.ac.uk/pdbsum/2y9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y9x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PPO3_AGABI PPO3_AGABI]] Copper-containing oxidase that catalyzes both the o-hydroxylation of monophenols and the subsequent oxidation of the resulting o-diphenols into reactive o-quinones, which evolve spontaneously to produce intermediates, which associate in dark brown pigments. Involved in the initial step of melanin synthesis. Melanins constitute a mechanism of defense and resistance to stress such as UV radiations, free radicals, gamma rays, dehydratation and extreme temperatures, and contribute to the fungal cell-wall resistance against hydrolytic enzymes in avoiding cellular lysis. Fungal pigments are also involved in the formation and stability of spores (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Tyrosinase|Tyrosinase]] | *[[Tyrosinase 3D structures|Tyrosinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> |