3hd0
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3hd0 is ON HOLD Authors: Utepbergenov, Darkhan, Cooper, David R., Derewenda, Urszula, Derewenda, Zygmunt S. Description: Crystal structure of Tm186...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Tm1865, an Endonuclease V from Thermotoga Maritima== | |
| + | <StructureSection load='3hd0' size='340' side='right'caption='[[3hd0]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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='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> | ||
| + | == 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> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <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/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hd0 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Endonuclease 3D structures|Endonuclease 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga maritima]] | ||
| + | [[Category: Cooper DR]] | ||
| + | [[Category: Derewenda U]] | ||
| + | [[Category: Derewenda ZS]] | ||
| + | [[Category: Utepbergenov D]] | ||
Current revision
Crystal structure of Tm1865, an Endonuclease V from Thermotoga Maritima
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