View source for 5mkw


==Crystal structure of the human ZRANB3 HNH domain==
<StructureSection load='5mkw' size='340' side='right'caption='[[5mkw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mkw]] 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=5MKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MKW FirstGlance]. <br>
</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&#8491;</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5mkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkw OCA], [https://pdbe.org/5mkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mkw RCSB], [https://www.ebi.ac.uk/pdbsum/5mkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ZRAB3_HUMAN ZRAB3_HUMAN] DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.<ref>PMID:21078962</ref> <ref>PMID:22704558</ref> <ref>PMID:22705370</ref> <ref>PMID:22759634</ref> <ref>PMID:26884333</ref> 
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ariza A]]