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3hhs

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==Crystal Structure of Manduca sexta prophenoloxidase==
==Crystal Structure of Manduca sexta prophenoloxidase==
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<StructureSection load='3hhs' size='340' side='right' caption='[[3hhs]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
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<StructureSection load='3hhs' size='340' side='right'caption='[[3hhs]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3hhs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Carolina_sphinx Carolina sphinx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HHS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3hhs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HHS FirstGlance]. <br>
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</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></td></tr>
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</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></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosinase Tyrosinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.18.1 1.14.18.1] </span></td></tr>
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<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>
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<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=3hhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hhs OCA], [http://pdbe.org/3hhs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hhs RCSB], [http://www.ebi.ac.uk/pdbsum/3hhs PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hhs OCA], [https://pdbe.org/3hhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hhs RCSB], [https://www.ebi.ac.uk/pdbsum/3hhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hhs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PRP2_MANSE PRP2_MANSE]] This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization.<ref>PMID:16291091</ref> [[http://www.uniprot.org/uniprot/PRP1_MANSE PRP1_MANSE]] This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization.<ref>PMID:16291091</ref> <ref>PMID:9474780</ref>
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[[https://www.uniprot.org/uniprot/PRP2_MANSE PRP2_MANSE]] This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization.<ref>PMID:16291091</ref> [[https://www.uniprot.org/uniprot/PRP1_MANSE PRP1_MANSE]] This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization.<ref>PMID:16291091</ref> <ref>PMID:9474780</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/3hhs_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/3hhs_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Carolina sphinx]]
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[[Category: Large Structures]]
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[[Category: Manduca sexta]]
[[Category: Tyrosinase]]
[[Category: Tyrosinase]]
[[Category: Deng, J]]
[[Category: Deng, J]]

Current revision

Crystal Structure of Manduca sexta prophenoloxidase

PDB ID 3hhs

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