2xsn

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==Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain==
==Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain==
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<StructureSection load='2xsn' size='340' side='right' caption='[[2xsn]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
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<StructureSection load='2xsn' size='340' side='right'caption='[[2xsn]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xsn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XSN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xsn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XSN 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=ZN:ZINC+ION'>ZN</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]] 2.68&#8491;</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/Tyrosine_3-monooxygenase Tyrosine 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.2 1.14.16.2] </span></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=ZN:ZINC+ION'>ZN</scene></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=2xsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xsn RCSB], [http://www.ebi.ac.uk/pdbsum/2xsn PDBsum]</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=2xsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsn OCA], [https://pdbe.org/2xsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xsn RCSB], [https://www.ebi.ac.uk/pdbsum/2xsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xsn ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/TY3H_HUMAN TY3H_HUMAN]] Autosomal recessive dopa-responsive dystonia. The disease is caused by mutations affecting the gene represented in this entry. May play a role in the pathogenesis of Parkinson disease (PD). A genome-wide copy number variation analysis has identified a 34 kilobase deletion over the TH gene in a PD patient but not in any controls.<ref>PMID:20809526</ref>
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[https://www.uniprot.org/uniprot/TY3H_HUMAN TY3H_HUMAN] Autosomal recessive dopa-responsive dystonia. The disease is caused by mutations affecting the gene represented in this entry. May play a role in the pathogenesis of Parkinson disease (PD). A genome-wide copy number variation analysis has identified a 34 kilobase deletion over the TH gene in a PD patient but not in any controls.<ref>PMID:20809526</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TY3H_HUMAN TY3H_HUMAN]] Plays an important role in the physiology of adrenergic neurons.
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[https://www.uniprot.org/uniprot/TY3H_HUMAN TY3H_HUMAN] Plays an important role in the physiology of adrenergic neurons.
==See Also==
==See Also==
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*[[Tyrosine hydroxylase|Tyrosine hydroxylase]]
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*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
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*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Tyrosine 3-monooxygenase]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Cooper, C D.O]]
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[[Category: Cooper CDO]]
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[[Category: Delft, F Von]]
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[[Category: Edwards AM]]
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[[Category: Edwards, A M]]
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[[Category: Gileadi O]]
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[[Category: Gileadi, O]]
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[[Category: Kavanagh KL]]
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[[Category: Kavanagh, K L]]
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[[Category: Knapp S]]
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[[Category: Knapp, S]]
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[[Category: Krysztofinska E]]
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[[Category: Krysztofinska, E]]
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[[Category: Muniz JRC]]
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[[Category: Muniz, J R.C]]
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[[Category: Oppermann U]]
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[[Category: Oppermann, U]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J]]
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[[Category: Yue WW]]
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[[Category: Yue, W W]]
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[[Category: Von Delft F]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain

PDB ID 2xsn

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