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3u7e

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'''Unreleased structure'''
 
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The entry 3u7e is ON HOLD until sometime in the future
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==Crystal structure of mPNKP catalytic fragment (D170A)==
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<StructureSection load='3u7e' size='340' side='right'caption='[[3u7e]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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Authors: Coquelle, N., Havali, Z., Bernstein, N., Green, R., Glover, J.N.M.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3u7e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U7E FirstGlance]. <br>
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Description: Crystal structure of mPNKP catalytic fragment (D170A)
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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]] 1.7&#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=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3u7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u7e OCA], [https://pdbe.org/3u7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u7e RCSB], [https://www.ebi.ac.uk/pdbsum/3u7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u7e ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PNKP_MOUSE PNKP_MOUSE] Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone.
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Bernstein N]]
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[[Category: Coquelle N]]
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[[Category: Glover JNM]]
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[[Category: Green R]]
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[[Category: Havali Z]]

Current revision

Crystal structure of mPNKP catalytic fragment (D170A)

PDB ID 3u7e

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