4l1m

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'''Unreleased structure'''
 
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The entry 4l1m is ON HOLD
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==Structure of the first RCC1-like domain of HERC2==
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<StructureSection load='4l1m' size='340' side='right'caption='[[4l1m]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4l1m]] is a 3 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=4L1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L1M FirstGlance]. <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]] 2.6&#8491;</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=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></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=4l1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1m OCA], [https://pdbe.org/4l1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l1m RCSB], [https://www.ebi.ac.uk/pdbsum/4l1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l1m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HERC2_HUMAN HERC2_HUMAN] E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity.<ref>PMID:20023648</ref> <ref>PMID:20304803</ref> <ref>PMID:22508508</ref>
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Authors: Tempel, W., Khan, M.B., Dong, A., Hu, J., Li, Y., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Tong, Y., Structural Genomics Consortium (SGC)
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==See Also==
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
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Description: Structure of the first RCC1-like domain of HERC2
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra C]]
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[[Category: Dong A]]
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[[Category: Edwards AM]]
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[[Category: Hu J]]
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[[Category: Khan MB]]
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[[Category: Li Y]]
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[[Category: Tempel W]]
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[[Category: Tong Y]]

Current revision

Structure of the first RCC1-like domain of HERC2

PDB ID 4l1m

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