3whn
From Proteopedia
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| - | {{STRUCTURE_3whn| PDB=3whn | SCENE= }} | ||
| - | ===Hemerythrin-like domain of DcrH I119H mutant (met)=== | ||
| - | {{ABSTRACT_PUBMED_24400317}} | ||
| - | == | + | ==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]] 1.90Å' 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]] 1.9Å</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_DESVH Q726F3_DESVH] | ||
| + | <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. | ||
| - | + | 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 | + | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 3whn" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Desulfovibrio vulgaris str. Hildenborough]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Hayashi T]] |
| - | [[Category: | + | [[Category: Hirota S]] |
| - | [[Category: | + | [[Category: Kurtz Jr DM]] |
| + | [[Category: Okamoto Y]] | ||
| + | [[Category: Onoda A]] | ||
| + | [[Category: Shiro Y]] | ||
| + | [[Category: Sugimoto H]] | ||
| + | [[Category: Takano Y]] | ||
Current revision
Hemerythrin-like domain of DcrH I119H mutant (met)
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