2yyl

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==Crystal structure of the mutant of HpaB (T198I, A276G, and R466H) complexed with FAD==
==Crystal structure of the mutant of HpaB (T198I, A276G, and R466H) complexed with FAD==
<StructureSection load='2yyl' size='340' side='right' caption='[[2yyl]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='2yyl' size='340' side='right' caption='[[2yyl]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2yyl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YYL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2yyl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YYL FirstGlance]. <br>
</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yyg|2yyg]], [[2yyi|2yyi]], [[2yyj|2yyj]], [[2yyk|2yyk]], [[2yym|2yym]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yyg|2yyg]], [[2yyi|2yyi]], [[2yyj|2yyj]], [[2yyk|2yyk]], [[2yym|2yym]]</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/4-hydroxyphenylacetate_3-monooxygenase 4-hydroxyphenylacetate 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.3 1.14.13.3] </span></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/4-hydroxyphenylacetate_3-monooxygenase 4-hydroxyphenylacetate 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.9 1.14.14.9] </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=2yyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yyl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yyl RCSB], [http://www.ebi.ac.uk/pdbsum/2yyl PDBsum]</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=2yyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yyl OCA], [http://pdbe.org/2yyl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yyl RCSB], [http://www.ebi.ac.uk/pdbsum/2yyl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yyl ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HPAB_THET8 HPAB_THET8]] Utilizes FADH(2) supplied by HpaC, to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA).<ref>PMID:17804419</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2yyl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2yyl" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: 4-hydroxyphenylacetate 3-monooxygenase]]
[[Category: 4-hydroxyphenylacetate 3-monooxygenase]]
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[[Category: Thermus thermophilus hb8]]
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[[Category: Thet8]]
[[Category: Ebihara, A]]
[[Category: Ebihara, A]]
[[Category: Hisano, T]]
[[Category: Hisano, T]]

Revision as of 16:34, 11 August 2016

Crystal structure of the mutant of HpaB (T198I, A276G, and R466H) complexed with FAD

2yyl, resolution 1.75Å

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