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4fh1

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==S. cerevisiae Ubc13-N79A==
==S. cerevisiae Ubc13-N79A==
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<StructureSection load='4fh1' size='340' side='right' caption='[[4fh1]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
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<StructureSection load='4fh1' size='340' side='right'caption='[[4fh1]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fh1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FH1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FH1 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=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene></td></tr>
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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]] 2.61&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBC13, YDR092W, YD6652.04 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=4fh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fh1 OCA], [https://pdbe.org/4fh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fh1 RCSB], [https://www.ebi.ac.uk/pdbsum/4fh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fh1 ProSAT]</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=4fh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fh1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fh1 RCSB], [http://www.ebi.ac.uk/pdbsum/4fh1 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/UBC13_YEAST UBC13_YEAST]] Has a role in the DNA error-free postreplication repair (PRR) pathway. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'.
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[https://www.uniprot.org/uniprot/UBC13_YEAST UBC13_YEAST] Has a role in the DNA error-free postreplication repair (PRR) pathway. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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It is widely accepted that ubiquitin-conjugating enzymes contain an active site asparagine that serves as an oxyanion hole, thereby stabilizing a negatively charged transition state intermediate and promoting ubiquitin transfer. Using structural and biochemical approaches to study the role of the conserved asparagine to ubiquitin conjugation by Ubc13-Mms2, we conclude that the importance of this residue stems primarily from its structural role in stabilizing an active site loop.
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A conserved asparagine has a structural role in ubiquitin-conjugating enzymes.,Berndsen CE, Wiener R, Yu IW, Ringel AE, Wolberger C Nat Chem Biol. 2013 Mar;9(3):154-6. doi: 10.1038/nchembio.1159. Epub 2013 Jan 6. PMID:23292652<ref>PMID:23292652</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Ubiquitin conjugating enzyme|Ubiquitin conjugating enzyme]]
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*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Saccharomyces cerevisiae s288c]]
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[[Category: Large Structures]]
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[[Category: Ubiquitin--protein ligase]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Berndsen, C E]]
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[[Category: Berndsen CE]]
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[[Category: Wiener, R]]
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[[Category: Wiener R]]
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[[Category: Wolberger, C]]
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[[Category: Wolberger C]]
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[[Category: Ligase]]
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[[Category: Ubiquitin conjugating enzyme]]
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Current revision

S. cerevisiae Ubc13-N79A

PDB ID 4fh1

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