3hd0: Difference between revisions

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<StructureSection load='3hd0' size='340' side='right'caption='[[3hd0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='3hd0' size='340' side='right'caption='[[3hd0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3hd0]] is a 3 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=3HD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HD0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3hd0]] is a 3 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=3HD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HD0 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nfi, TM_1865 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3hd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hd0 OCA], [https://pdbe.org/3hd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hd0 RCSB], [https://www.ebi.ac.uk/pdbsum/3hd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hd0 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=3hd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hd0 OCA], [https://pdbe.org/3hd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hd0 RCSB], [https://www.ebi.ac.uk/pdbsum/3hd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hd0 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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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/3hd0_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/3hd0_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Deoxyribonuclease V]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cooper, D R]]
[[Category: Thermotoga maritima]]
[[Category: Derewenda, U]]
[[Category: Cooper DR]]
[[Category: Derewenda, Z S]]
[[Category: Derewenda U]]
[[Category: ISFI, Integrated Center for Structure and Function Innovation]]
[[Category: Derewenda ZS]]
[[Category: Utepbergenov, D]]
[[Category: Utepbergenov D]]
[[Category: Cytoplasm]]
[[Category: Dna damage]]
[[Category: Dna repair]]
[[Category: Endonuclease]]
[[Category: Endonuclease v]]
[[Category: Hydrolase]]
[[Category: Integrated center for structure and function innovation]]
[[Category: Isfi]]
[[Category: Magnesium]]
[[Category: Nuclease]]
[[Category: PSI, Protein structure initiative]]
[[Category: Rnaseh superfamily]]
[[Category: Structural genomic]]

Latest revision as of 09:13, 30 October 2024

Crystal structure of Tm1865, an Endonuclease V from Thermotoga Maritima

3hd0, resolution 2.70Å

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