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1n56

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Current revision (07:19, 25 October 2023) (edit) (undo)
 
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<StructureSection load='1n56' size='340' side='right'caption='[[1n56]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1n56' size='340' side='right'caption='[[1n56]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1n56]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N56 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1n56]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus] 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=1N56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N56 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.4&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></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=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jx4|1jx4]], [[1jxl|1jxl]], [[1n48|1n48]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dpo4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</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=1n56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n56 OCA], [https://pdbe.org/1n56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n56 RCSB], [https://www.ebi.ac.uk/pdbsum/1n56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n56 ProSAT]</span></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=1n56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n56 OCA], [https://pdbe.org/1n56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n56 RCSB], [https://www.ebi.ac.uk/pdbsum/1n56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n56 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DPO4_SULSO DPO4_SULSO]] Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. It is involved in translesional synthesis.[HAMAP-Rule:MF_01113]
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[https://www.uniprot.org/uniprot/DPO4_SACS2 DPO4_SACS2] Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. It is involved in translesional synthesis.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 1n56" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1n56" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 35091]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Boudsocq, F]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Ling, H]]
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[[Category: Synthetic construct]]
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[[Category: Woodgate, R]]
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[[Category: Boudsocq F]]
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[[Category: Yang, W]]
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[[Category: Ling H]]
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[[Category: Dna lesion bypass]]
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[[Category: Woodgate R]]
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[[Category: Dna polymerase]]
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[[Category: Yang W]]
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[[Category: Protein-dna complex]]
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[[Category: Transferase-dna complex]]
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[[Category: Y-family]]
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Current revision

Y-family DNA polymerase Dpo4 in complex with DNA containing abasic lesion

PDB ID 1n56

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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