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==Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme==
==Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme==
<StructureSection load='3rii' size='340' side='right' caption='[[3rii]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3rii' size='340' side='right'caption='[[3rii]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3rii]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RII FirstGlance]. <br>
<table><tr><td colspan='2'>[[3rii]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RII FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.0008&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ihr|3ihr]]</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=3rii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rii OCA], [https://pdbe.org/3rii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rii RCSB], [https://www.ebi.ac.uk/pdbsum/3rii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rii ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AD-019, CGI-70, UCH37, UCHL5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
</table>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=3rii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rii OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rii RCSB], [http://www.ebi.ac.uk/pdbsum/3rii PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme.,Maiti TK, Permaul M, Boudreaux DA, Mahanic C, Mauney S, Das C FEBS J. 2011 Oct 13. doi: 10.1111/j.1742-4658.2011.08393.x. PMID:21995438<ref>PMID:21995438</ref>
Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme.,Maiti TK, Permaul M, Boudreaux DA, Mahanic C, Mauney S, Das C FEBS J. 2011 Oct 13. doi: 10.1111/j.1742-4658.2011.08393.x. PMID:21995438<ref>PMID:21995438</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3rii" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Thioesterase|Thioesterase]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Large Structures]]
[[Category: Das, C.]]
[[Category: Das C]]
[[Category: Alpha-beta-alpha fold]]
[[Category: Cysteine protease]]
[[Category: Deubiquitinating enzyme]]
[[Category: Hydrolase]]
[[Category: Thiol hydroalse]]
[[Category: Ubiquitin hydrolase]]
Retrieved from "https://proteopedia.org/3rii"