2w36: Difference between revisions

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<StructureSection load='2w36' size='340' side='right'caption='[[2w36]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2w36' size='340' side='right'caption='[[2w36]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2w36]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W36 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2w36]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] 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=2W36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W36 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene>, <scene name='pdbligand=DI:2-DEOXYINOSINE-5-MONOPHOSPHATE'>DI</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2w35|2w35]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Deoxyribonuclease_V Deoxyribonuclease V], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.7 3.1.21.7] </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=2w36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w36 OCA], [https://pdbe.org/2w36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w36 RCSB], [https://www.ebi.ac.uk/pdbsum/2w36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w36 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=2w36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w36 OCA], [https://pdbe.org/2w36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w36 RCSB], [https://www.ebi.ac.uk/pdbsum/2w36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w36 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NFI_THEMA NFI_THEMA]] Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. Acts in DNA repair. In vitro, can also cleave single-stranded substrates with inosine, double-stranded DNA with apurinic sites, or DNA sites with uracil or a mismatched base. When present in molar excess, two protein molecules can bind to the same DNA substrate and effect cleavage of both strands (in vitro).<ref>PMID:12081482</ref>
[https://www.uniprot.org/uniprot/NFI_THEMA NFI_THEMA] Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. Acts in DNA repair. In vitro, can also cleave single-stranded substrates with inosine, double-stranded DNA with apurinic sites, or DNA sites with uracil or a mismatched base. When present in molar excess, two protein molecules can bind to the same DNA substrate and effect cleavage of both strands (in vitro).<ref>PMID:12081482</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Deoxyribonuclease V]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Alseth, I]]
[[Category: Synthetic construct]]
[[Category: Arvai, A S]]
[[Category: Thermotoga maritima]]
[[Category: Backe, P H]]
[[Category: Alseth I]]
[[Category: Bjoras, M]]
[[Category: Arvai AS]]
[[Category: Cao, W]]
[[Category: Backe PH]]
[[Category: Dalhus, B]]
[[Category: Bjoras M]]
[[Category: Gao, H]]
[[Category: Cao W]]
[[Category: Olsen, O E]]
[[Category: Dalhus B]]
[[Category: Rosnes, I]]
[[Category: Gao H]]
[[Category: Tainer, J A]]
[[Category: Olsen OE]]
[[Category: Dna damage]]
[[Category: Rosnes I]]
[[Category: Dna repair]]
[[Category: Tainer JA]]
[[Category: Endonuclease]]
[[Category: Endonucleasev]]
[[Category: Hydrolase]]
[[Category: Hypoxanthine]]
[[Category: Inosine]]
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