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3sxx

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==Hansenula polymorpha copper amine oxidase-1 in complex with Co(II)==
==Hansenula polymorpha copper amine oxidase-1 in complex with Co(II)==
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<StructureSection load='3sxx' size='340' side='right' caption='[[3sxx]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
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<StructureSection load='3sxx' size='340' side='right'caption='[[3sxx]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sxx]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ogataea_angusta Ogataea angusta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SXX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sxx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ogataea_angusta Ogataea angusta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SXX 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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.27&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a2v|1a2v]], [[2oov|2oov]], [[3sx1|3sx1]]</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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AMO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=870730 Ogataea angusta])</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=3sxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sxx OCA], [https://pdbe.org/3sxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sxx RCSB], [https://www.ebi.ac.uk/pdbsum/3sxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sxx ProSAT]</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/Primary-amine_oxidase Primary-amine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.21 1.4.3.21] </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=3sxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sxx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sxx RCSB], [http://www.ebi.ac.uk/pdbsum/3sxx PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/AMO_PICAN AMO_PICAN]
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Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their corresponding aldehydes, with the concomitant reduction of O(2) to H(2)O(2). Catalysis requires two cofactors: a mononuclear copper center and the cofactor 2,4,5-trihydroxyphenylalanine quinone (TPQ). TPQ is synthesized through the post-translational modification of an endogenous tyrosine residue and requires only oxygen and copper to proceed. TPQ biogenesis in CAO can be supported by alternate metals, albeit at decreased rates. A variety of factors are thought to contribute to the degree to which a metal can support TPQ biogenesis, including Lewis acidity, redox potential and electrostatic stabilization capability. The crystal structure has been solved of one of two characterized CAOs from the yeast Hansenula polymorpha (HPAO-1) in its metal-free (apo) form, which contains an unmodified precursor tyrosine residue instead of fully processed TPQ (HPAO-1 was denoted HPAO in the literature prior to 2010). Structures of apoHPAO-1 in complex with Cu(I) and Co(II) have also been solved, providing structural insight into metal binding prior to biogenesis.
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The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with CuI and CoII.,Klema VJ, Johnson BJ, Klinman JP, Wilmot CM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):501-10., doi: 10.1107/S1744309112012857. Epub 2012 Apr 20. PMID:22691777<ref>PMID:22691777</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Copper Amine Oxidase|Copper Amine Oxidase]]
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*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Ogataea angusta]]
[[Category: Ogataea angusta]]
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[[Category: Primary-amine oxidase]]
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[[Category: Klema VJ]]
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[[Category: Klema, V J]]
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[[Category: Wilmot CM]]
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[[Category: Wilmot, C M]]
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[[Category: Oxidoreductase]]
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[[Category: Peroxisome]]
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Current revision

Hansenula polymorpha copper amine oxidase-1 in complex with Co(II)

PDB ID 3sxx

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