4mah: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mah]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MAH FirstGlance]. <br> | <table><tr><td colspan='2'>[[4mah]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MAH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.55Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4mah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mah OCA], [https://pdbe.org/4mah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mah RCSB], [https://www.ebi.ac.uk/pdbsum/4mah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mah 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=4mah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mah OCA], [https://pdbe.org/4mah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mah RCSB], [https://www.ebi.ac.uk/pdbsum/4mah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mah ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/LP11_ASPOR LP11_ASPOR] Lytic polysaccharide monooxygenase (LPMO) that depolymerizes chitin via the oxidation of scissile beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (PubMed:24362702). 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:24362702). Active on chitin but has no activity on other substrates, including diverse mannans, cellulose and starch (data not shown) (PubMed:24362702). Primary chain cleavage yields predominantly aldonic acid oligosaccharides with even-numbered degrees of polymerization (PubMed:24362702).<ref>PMID:24362702</ref> | ||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||