1e8g

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==STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL==
==STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL==
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<StructureSection load='1e8g' size='340' side='right' caption='[[1e8g]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='1e8g' size='340' side='right'caption='[[1e8g]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1e8g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10495 Atcc 10495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E8G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1e8g]] 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=1E8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E8G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCR:ALPHA,ALPHA,ALPHA-TRIFLUORO-P-CRESOL'>FCR</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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e8f|1e8f]], [[1e8h|1e8h]], [[1ahu|1ahu]], [[1ahv|1ahv]], [[1ahz|1ahz]], [[1dzn|1dzn]], [[1e0y|1e0y]], [[1qlt|1qlt]], [[1qlu|1qlu]], [[1vao|1vao]], [[2vao|2vao]]</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCR:ALPHA,ALPHA,ALPHA-TRIFLUORO-P-CRESOL'>FCR</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Vanillyl-alcohol_oxidase Vanillyl-alcohol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.38 1.1.3.38] </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=1e8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8g OCA], [https://pdbe.org/1e8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e8g RCSB], [https://www.ebi.ac.uk/pdbsum/1e8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8g ProSAT]</span></td></tr>
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<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=1e8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8g OCA], [http://pdbe.org/1e8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e8g RCSB], [http://www.ebi.ac.uk/pdbsum/1e8g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8g ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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</div>
</div>
<div class="pdbe-citations 1e8g" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1e8g" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Vanillyl-alcohol oxidase|Vanillyl-alcohol oxidase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 10495]]
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[[Category: Large Structures]]
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[[Category: Vanillyl-alcohol oxidase]]
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[[Category: Penicillium simplicissimum]]
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[[Category: Fraaije, M W]]
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[[Category: Fraaije MW]]
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[[Category: Mattevi, A]]
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[[Category: Mattevi A]]
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[[Category: Flavoenzyme]]
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[[Category: Oxidoreductase]]
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[[Category: Specificity]]
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Current revision

STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL

PDB ID 1e8g

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