4udp: Difference between revisions
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New page: '''Unreleased structure''' The entry 4udp is ON HOLD Authors: Dijkman, W., Binda, C., Fraaije, M., Mattevi, A. Description: |
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==Crystal structure of 5-hydroxymethylfurfural oxidase (HMFO) in the oxidized state== | |||
<StructureSection load='4udp' size='340' side='right'caption='[[4udp]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4udp]] 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=4UDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UDP 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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=4udp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4udp OCA], [https://pdbe.org/4udp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4udp RCSB], [https://www.ebi.ac.uk/pdbsum/4udp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4udp 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]] | |||
