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{{STRUCTURE_3whn|  PDB=3whn  |  SCENE=  }}
===Hemerythrin-like domain of DcrH I119H mutant (met)===
{{ABSTRACT_PUBMED_24400317}}


==About this Structure==
==Hemerythrin-like domain of DcrH I119H mutant (met)==
[[3whn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WHN OCA].  
<StructureSection load='3whn' size='340' side='right'caption='[[3whn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3whn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WHN 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFO:CHLORO+DIIRON-OXO+MOIETY'>CFO</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=3whn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3whn OCA], [https://pdbe.org/3whn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3whn RCSB], [https://www.ebi.ac.uk/pdbsum/3whn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3whn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q726F3_NITV2 Q726F3_NITV2]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The O2-binding carboxylate-bridged diiron site in DcrH-Hr was engineered in an effort to perform the H2O2-dependent oxidation of external substrates. A His residue was introduced near the diiron site in place of a conserved residue, Ile119. The I119H variant promotes the oxidation of guaiacol and 1,4-cyclohexadiene upon addition of H2O2.


==Reference==
HO-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin.,Okamoto Y, Onoda A, Sugimoto H, Takano Y, Hirota S, Kurtz DM, Shiro Y, Hayashi T Chem Commun (Camb). 2014 Jan 8. PMID:24400317<ref>PMID:24400317</ref>
<ref group="xtra">PMID:024400317</ref><references group="xtra"/><references/>
 
[[Category: Hayashi, T.]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Hirota, S.]]
</div>
[[Category: Kurtz, D M.]]
<div class="pdbe-citations 3whn" style="background-color:#fffaf0;"></div>
[[Category: Okamoto, Y.]]
== References ==
[[Category: Onoda, A.]]
<references/>
[[Category: Shiro, Y.]]
__TOC__
[[Category: Sugimoto, H.]]
</StructureSection>
[[Category: Takano, Y.]]
[[Category: Desulfovibrio vulgaris str. Hildenborough]]
[[Category: Helix bundle]]
[[Category: Large Structures]]
[[Category: Metal binding protein]]
[[Category: Hayashi T]]
[[Category: Metal-binding]]
[[Category: Hirota S]]
[[Category: Oxygen sensor]]
[[Category: Kurtz Jr DM]]
[[Category: Okamoto Y]]
[[Category: Onoda A]]
[[Category: Shiro Y]]
[[Category: Sugimoto H]]
[[Category: Takano Y]]
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