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5lbn
From Proteopedia
(Difference between revisions)
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<StructureSection load='5lbn' size='340' side='right'caption='[[5lbn]], [[Resolution|resolution]] 1.42Å' scene=''> | <StructureSection load='5lbn' size='340' side='right'caption='[[5lbn]], [[Resolution|resolution]] 1.42Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5lbn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LBN OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5lbn]] is a 1 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=5LBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LBN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.42Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5lbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbn OCA], [https://pdbe.org/5lbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lbn RCSB], [https://www.ebi.ac.uk/pdbsum/5lbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/UB2E1_HUMAN UB2E1_HUMAN] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination.<ref>PMID:16428300</ref> <ref>PMID:20061386</ref> |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Anandapadamanaban | + | [[Category: Anandapadamanaban M]] |
| - | [[Category: Moche | + | [[Category: Moche M]] |
| - | [[Category: Sunnerhagen | + | [[Category: Sunnerhagen M]] |
| - | + | ||
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Revision as of 16:14, 4 October 2023
High-resolution crystal structure of the UBC core domain of UBE2E1/UbcH6
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