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3pih
From Proteopedia
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==T. maritima UvrA in complex with fluorescein-modified DNA== | ==T. maritima UvrA in complex with fluorescein-modified DNA== | ||
| - | <StructureSection load='3pih' size='340' side='right' caption='[[3pih]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='3pih' size='340' side='right'caption='[[3pih]], [[Resolution|resolution]] 2.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3pih]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3pih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PIH FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pih OCA], [https://pdbe.org/3pih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pih RCSB], [https://www.ebi.ac.uk/pdbsum/3pih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pih ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/UVRA_THEMA UVRA_THEMA] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (By similarity). |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3pih" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Jaciuk | + | [[Category: Jaciuk M]] |
| - | [[Category: Nowak | + | [[Category: Nowak E]] |
| - | [[Category: Nowotny | + | [[Category: Nowotny M]] |
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Current revision
T. maritima UvrA in complex with fluorescein-modified DNA
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