View source for 9hdg


==The structure of the catalytic domain of AfAA11B from the filamentous fungus Aspergillus fumigatus==
<StructureSection load='9hdg' size='340' side='right'caption='[[9hdg]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9hdg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HDG 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]] 1.26&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9hdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hdg OCA], [https://pdbe.org/9hdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hdg RCSB], [https://www.ebi.ac.uk/pdbsum/9hdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hdg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LP11B_ASPFU LP11B_ASPFU] Lytic polysaccharide monooxygenase (LPMO)-like protein that acts as a strict peroxygenase and does not catalyze a monooxygenase reaction (PubMed:34567832). It is indeed hardly active on chitin, while being very active on soluble oligomers of N-acetylglucosamine (PubMed:34567832). Cleaves the glycosidic bonds byoxidizing the C1 position (PubMed:34567832). Also unable to oxidize cellopentaose (PubMed:34738811). Probably breaks glycosidic bonds in non-polymeric substrates possibly carbohydrates in the cell wall of the fungus or its competitors (PubMed:34567832). In the presence of chitotetraose, the enzyme can withstand considerable amounts of H(2)O(2), which it uses to efficiently and stoichiometrically convert this substrate (PubMed:34567832).<ref>PMID:34567832</ref> <ref>PMID:34738811</ref> 
== References ==
<references/>
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</StructureSection>
[[Category: Aspergillus fumigatus]]
[[Category: Large Structures]]
[[Category: Ayuso-Fernandez I]]
[[Category: Eijsink VGH]]
[[Category: Emrich-Mills T]]
[[Category: Englund AN]]
[[Category: Gautieri A]]
[[Category: Golten O]]
[[Category: Hall K]]
[[Category: Kjendseth AR]]
[[Category: Landsem E]]
[[Category: Rieder L]]
[[Category: Roennekleiv SE]]
[[Category: Skaali R]]
[[Category: Soerlie M]]