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3zvm

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==The structural basis for substrate recognition by mammalian polynucleotide kinase 3' phosphatase==
==The structural basis for substrate recognition by mammalian polynucleotide kinase 3' phosphatase==
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<StructureSection load='3zvm' size='340' side='right' caption='[[3zvm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3zvm' size='340' side='right'caption='[[3zvm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3zvm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZVM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3zvm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZVM 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.997&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ujx|1ujx]], [[3zvl|3zvl]], [[1yj5|1yj5]], [[1yjm|1yjm]], [[3zvn|3zvn]]</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3zvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zvm OCA], [http://pdbe.org/3zvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zvm RCSB], [http://www.ebi.ac.uk/pdbsum/3zvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zvm ProSAT]</span></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=3zvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zvm OCA], [https://pdbe.org/3zvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zvm RCSB], [https://www.ebi.ac.uk/pdbsum/3zvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zvm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Garces, F]]
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[[Category: Mus musculus]]
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[[Category: Oliver, A W]]
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[[Category: Synthetic construct]]
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[[Category: Pearl, L H]]
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[[Category: Garces F]]
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[[Category: Base excision repair]]
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[[Category: Oliver AW]]
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[[Category: Ber]]
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[[Category: Pearl LH]]
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[[Category: Cancer]]
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[[Category: Dna repair]]
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[[Category: Hydrolase-transferase-dna complex]]
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[[Category: Nhej]]
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[[Category: Non-homologous end-joining]]
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Current revision

The structural basis for substrate recognition by mammalian polynucleotide kinase 3' phosphatase

PDB ID 3zvm

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