5knl

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==Crystal structure of S. pombe ubiquitin E1 (Uba1) in complex with Ubc15 and ubiquitin==
==Crystal structure of S. pombe ubiquitin E1 (Uba1) in complex with Ubc15 and ubiquitin==
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<StructureSection load='5knl' size='340' side='right' caption='[[5knl]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='5knl' size='340' side='right'caption='[[5knl]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5knl]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KNL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KNL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5knl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Moesziomyces_antarcticus Moesziomyces antarcticus] and [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KNL 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=SO4:SULFATE+ION'>SO4</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]] 2.5&#8491;</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/E1_ubiquitin-activating_enzyme E1 ubiquitin-activating enzyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.45 6.2.1.45] </span></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=SO4:SULFATE+ION'>SO4</scene></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=5knl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5knl OCA], [http://pdbe.org/5knl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5knl RCSB], [http://www.ebi.ac.uk/pdbsum/5knl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5knl ProSAT]</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=5knl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5knl OCA], [https://pdbe.org/5knl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5knl RCSB], [https://www.ebi.ac.uk/pdbsum/5knl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5knl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/UBA1_SCHPO UBA1_SCHPO]] Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP. [[http://www.uniprot.org/uniprot/UBC15_SCHPO UBC15_SCHPO]] Catalyzes the covalent attachment of ubiquitin to other proteins. Has a role in the formation of chromatin structures that influence the localization of transcriptional silencing factors.[PROSITE-ProRule:PRU00388]<ref>PMID:12456009</ref>
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[https://www.uniprot.org/uniprot/UBA1_SCHPO UBA1_SCHPO] Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5knl" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5knl" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[3D structures of Ubiquitin activating enzyme|3D structures of Ubiquitin activating enzyme]]
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*[[3D structures of ubiquitin|3D structures of ubiquitin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: E1 ubiquitin-activating enzyme]]
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[[Category: Large Structures]]
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[[Category: Lv, Z]]
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[[Category: Moesziomyces antarcticus]]
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[[Category: Olsen, S K]]
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[[Category: Schizosaccharomyces pombe 972h-]]
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[[Category: Williams, K]]
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[[Category: Lv Z]]
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[[Category: Yuan, L]]
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[[Category: Olsen SK]]
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[[Category: Adenylation]]
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[[Category: Williams K]]
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[[Category: Atp-binding]]
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[[Category: Yuan L]]
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[[Category: Conformational change]]
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[[Category: E1]]
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[[Category: E2]]
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[[Category: Ligase]]
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[[Category: Thioester]]
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[[Category: Uba1]]
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[[Category: Ubc15]]
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[[Category: Ubiquitin]]
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[[Category: Ubiquitin e2 binding]]
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[[Category: Ubiquitination]]
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Current revision

Crystal structure of S. pombe ubiquitin E1 (Uba1) in complex with Ubc15 and ubiquitin

PDB ID 5knl

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