4udr
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the H467A mutant of 5-hydroxymethylfurfural oxidase (HMFO)== | |
| - | + | <StructureSection load='4udr' size='340' side='right'caption='[[4udr]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4udr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylovorus_sp._MP688 Methylovorus sp. MP688]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UDR 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]] 1.6Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=4udr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4udr OCA], [https://pdbe.org/4udr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4udr RCSB], [https://www.ebi.ac.uk/pdbsum/4udr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4udr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HMFO_METS6 HMFO_METS6] Involved in the degradation and detoxification of 5-(hydroxymethyl)furfural (HMF) by mediating its oxidation to furan-2,5-dicarboxylate (FDCA), a biobased platform chemical for the production of polymers. Active with a wide range of aromatic and aliphatic primary alcohols and aldehydes: acts on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation (PubMed:24271187, PubMed:24802551). To a lesser extent, is also able to catalyze the oxidation of thiols that are structurally similar to its alcohol substrates, yielding the corresponding thiocarbonyls (PubMed:25284255).<ref>PMID:24271187</ref> <ref>PMID:24802551</ref> <ref>PMID:25284255</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methylovorus sp. MP688]] | ||
| + | [[Category: Binda C]] | ||
| + | [[Category: Dijkman W]] | ||
| + | [[Category: Fraaije M]] | ||
| + | [[Category: Mattevi A]] | ||
Current revision
Crystal structure of the H467A mutant of 5-hydroxymethylfurfural oxidase (HMFO)
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