5d0i

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<StructureSection load='5d0i' size='340' side='right'caption='[[5d0i]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5d0i' size='340' side='right'caption='[[5d0i]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5d0i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D0I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D0I FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5d0i]] 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=5D0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D0I 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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d0k|5d0k]], [[5d0m|5d0m]]</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNF165 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5d0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d0i OCA], [https://pdbe.org/5d0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d0i RCSB], [https://www.ebi.ac.uk/pdbsum/5d0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d0i 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=5d0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d0i OCA], [http://pdbe.org/5d0i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d0i RCSB], [http://www.ebi.ac.uk/pdbsum/5d0i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d0i ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/RN165_HUMAN RN165_HUMAN]
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RING-domain E3 ligases enhance transfer of ubiquitin to substrate proteins by stabilizing the RING-bound thioester-linked E2 approximately ubiquitin conjugate in a defined conformation that primes the active site for nucleophilic attack. Here we report that the monomeric RING domains from the human E3 ligases Arkadia and Ark2C bind directly to free ubiquitin with an affinity comparable to that of other dedicated ubiquitin-binding domains. Further work showed that the Ark-like RING domain and the noncovalently bound ubiquitin molecule coordinately stabilize the E2-conjugated ubiquitin (donor ubiquitin) in the 'closed' conformation. Our studies identify the RING domain of Arkadia as a ubiquitin-binding domain and provide insight into a new ubiquitin-dependent mechanism used by monomeric RING domains to activate ubiquitin transfer. This study also suggests how substrates that have been monoubiquitinated could be favored for further ubiquitination.
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Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase activity.,Wright JD, Mace PD, Day CL Nat Struct Mol Biol. 2015 Dec 14. doi: 10.1038/nsmb.3142. PMID:26656854<ref>PMID:26656854</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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<div class="pdbe-citations 5d0i" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Day, C L]]
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[[Category: Day CL]]
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[[Category: Mace, P D]]
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[[Category: Mace PD]]
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[[Category: Wright, J D]]
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[[Category: Wright JD]]
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[[Category: Metal binding protein]]
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[[Category: Ring finger protein]]
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Current revision

Structure of RING finger protein 165

PDB ID 5d0i

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