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2y5b

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==Structure of USP21 in complex with linear diubiquitin-aldehyde==
==Structure of USP21 in complex with linear diubiquitin-aldehyde==
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<StructureSection load='2y5b' size='340' side='right' caption='[[2y5b]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='2y5b' size='340' side='right'caption='[[2y5b]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2y5b]] is a 4 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=2Y5B OCA]. <br>
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<table><tr><td colspan='2'>[[2y5b]] is a 4 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=2Y5B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y5B FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLZ:AMINO-ACETALDEHYDE'>GLZ</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLZ:AMINO-ACETALDEHYDE'>GLZ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2y5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y5b OCA], [https://pdbe.org/2y5b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y5b RCSB], [https://www.ebi.ac.uk/pdbsum/2y5b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y5b ProSAT]</span></td></tr>
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<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=2y5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y5b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y5b RCSB], [http://www.ebi.ac.uk/pdbsum/2y5b PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[https://www.uniprot.org/uniprot/UBP21_HUMAN UBP21_HUMAN] Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination (By similarity). Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates.<ref>PMID:10799498</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21.,Ye Y, Akutsu M, Reyes-Turcu F, Enchev RI, Wilkinson KD, Komander D EMBO Rep. 2011 Apr;12(4):350-7. Epub 2011 Mar 11. PMID:21399617<ref>PMID:21399617</ref>
Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21.,Ye Y, Akutsu M, Reyes-Turcu F, Enchev RI, Wilkinson KD, Komander D EMBO Rep. 2011 Apr;12(4):350-7. Epub 2011 Mar 11. PMID:21399617<ref>PMID:21399617</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2y5b" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Akutsu, M.]]
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[[Category: Large Structures]]
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[[Category: Enchev, R I.]]
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[[Category: Akutsu M]]
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[[Category: Komander, D.]]
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[[Category: Enchev RI]]
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[[Category: Reyes-Turcu, F.]]
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[[Category: Komander D]]
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[[Category: Wilkinson, K D.]]
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[[Category: Reyes-Turcu F]]
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[[Category: Ye, Y.]]
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[[Category: Wilkinson KD]]
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[[Category: Cell signaling]]
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[[Category: Ye Y]]
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[[Category: Isg15]]
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[[Category: Nedd8]]
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[[Category: Protein binding-hydrolase complex]]
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[[Category: Ubiquitin]]
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[[Category: Ubiquitin specific protease]]
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[[Category: Usp]]
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Current revision

Structure of USP21 in complex with linear diubiquitin-aldehyde

PDB ID 2y5b

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