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==Extended catalytic domain of Hypocrea jecorina LPMO 9A.==
==Extended catalytic domain of Hypocrea jecorina LPMO 9A.==
<StructureSection load='5o2w' size='340' side='right' caption='[[5o2w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5o2w' size='340' side='right'caption='[[5o2w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5o2w]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O2W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O2W FirstGlance]. <br>
<table><tr><td colspan='2'>[[5o2w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei_QM6a Trichoderma reesei QM6a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O2W FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5o2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o2w OCA], [http://pdbe.org/5o2w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o2w RCSB], [http://www.ebi.ac.uk/pdbsum/5o2w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o2w ProSAT]</span></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=5o2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o2w OCA], [https://pdbe.org/5o2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o2w RCSB], [https://www.ebi.ac.uk/pdbsum/5o2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o2w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LP9A_HYPJQ LP9A_HYPJQ] Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (PubMed:26285758, PubMed:28110665, PubMed:28900033, PubMed:30238672). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:28900033, PubMed:32414932, PubMed:34597668). Produces both neutral and oxidized cello-oligosaccharides from cellulose (PubMed:26285758, PubMed:28900033). Acts also on soluble cello-oligosaccharides as short as a tetramer (PubMed:26285758). The oxidative activity displays a synergistic effect capable of boosting endoglucanase activity, and thereby substrate depolymerization of soy cellulose by 27% (PubMed:28110665).<ref>PMID:26285758</ref> <ref>PMID:28110665</ref> <ref>PMID:28900033</ref> <ref>PMID:30238672</ref> <ref>PMID:32414932</ref> <ref>PMID:34597668</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5o2w" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5o2w" style="background-color:#fffaf0;"></div>
==See Also==
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hansson, H]]
[[Category: Large Structures]]
[[Category: Karkehabadi, S]]
[[Category: Trichoderma reesei QM6a]]
[[Category: Mikelssen, N E]]
[[Category: Hansson H]]
[[Category: Sandgren, M]]
[[Category: Karkehabadi S]]
[[Category: Metalloprotein]]
[[Category: Mikelssen NE]]
[[Category: Oxidoreductase]]
[[Category: Sandgren M]]
Retrieved from "https://proteopedia.org/5o2w"