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1e8h

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Current revision (11:56, 13 December 2023) (edit) (undo)
 
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<StructureSection load='1e8h' size='340' side='right'caption='[[1e8h]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1e8h' size='340' side='right'caption='[[1e8h]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1e8h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_10495 Atcc 10495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E8H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1e8h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E8H FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e8f|1e8f]], [[1e8g|1e8g]], [[1dzn|1dzn]], [[1e0y|1e0y]], [[1qlt|1qlt]], [[1qlu|1qlu]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aryl-alcohol_oxidase Aryl-alcohol oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.7 1.1.3.7] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8h OCA], [https://pdbe.org/1e8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e8h RCSB], [https://www.ebi.ac.uk/pdbsum/1e8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8h 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=1e8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8h OCA], [https://pdbe.org/1e8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e8h RCSB], [https://www.ebi.ac.uk/pdbsum/1e8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/VAOX_PENSI VAOX_PENSI]] Catalyzes the conversion of vanillin alcohol to vanillin, and also the conversion of a wide range of phenolic compounds bearing side chains of variable size at the para position of the aromatic ring. Crucial for the degradation of the secondary metabolites derived from the degradation of the lignin. Catalyzes besides the oxidation of 4-hydroxybenzyl alcohols, the oxidative deamination of 4-hydroxybenzylamines, the oxidative demethylation of 4-(methoxy-methyl)phenols and the oxidative hydration of 4-allylphenols. Most active with 4-allylphenols.
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[https://www.uniprot.org/uniprot/VAOX_PENSI VAOX_PENSI] Catalyzes the conversion of vanillin alcohol to vanillin, and also the conversion of a wide range of phenolic compounds bearing side chains of variable size at the para position of the aromatic ring. Crucial for the degradation of the secondary metabolites derived from the degradation of the lignin. Catalyzes besides the oxidation of 4-hydroxybenzyl alcohols, the oxidative deamination of 4-hydroxybenzylamines, the oxidative demethylation of 4-(methoxy-methyl)phenols and the oxidative hydration of 4-allylphenols. Most active with 4-allylphenols.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aryl-alcohol oxidase]]
 
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[[Category: Atcc 10495]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fraaije, M W]]
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[[Category: Penicillium simplicissimum]]
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[[Category: Mattevi, A]]
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[[Category: Fraaije MW]]
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[[Category: Catalysis]]
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[[Category: Mattevi A]]
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[[Category: Flavoenzyme]]
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[[Category: Flavoprotein]]
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[[Category: Methanol utilization]]
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[[Category: Oxidase]]
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[[Category: Oxidoreductase]]
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[[Category: Peroxisome]]
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Current revision

STRUCTURE OF THE H61T MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN THE APO FORM COMPLEXED BY ADP

PDB ID 1e8h

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OCA

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