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==The structure of human diamine oxidase complexed with an inhibitor aminoguanidine==
==The structure of human diamine oxidase complexed with an inhibitor aminoguanidine==
<StructureSection load='3mph' size='340' side='right' caption='[[3mph]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='3mph' size='340' side='right'caption='[[3mph]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3mph]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MPH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MPH FirstGlance]. <br>
<table><tr><td colspan='2'>[[3mph]] is a 2 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=3MPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MPH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGQ:3-[(3E)-3-(CARBAMIMIDOYLHYDRAZONO)-4-HYDROXY-6-OXOCYCLOHEXA-1,4-DIEN-1-YL]-L-ALANINE'>AGQ</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGQ:3-[(3E)-3-(CARBAMIMIDOYLHYDRAZONO)-4-HYDROXY-6-OXOCYCLOHEXA-1,4-DIEN-1-YL]-L-ALANINE'>AGQ</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hi7|3hi7]], [[3hig|3hig]], [[3hii|3hii]], [[3k5t|3k5t]]</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=3mph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mph OCA], [https://pdbe.org/3mph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mph RCSB], [https://www.ebi.ac.uk/pdbsum/3mph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mph ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diamine_oxidase Diamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.22 1.4.3.22] </span></td></tr>
<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=3mph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mph OCA], [http://pdbe.org/3mph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mph RCSB], [http://www.ebi.ac.uk/pdbsum/3mph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mph ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ABP1_HUMAN ABP1_HUMAN]] Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function.  
[https://www.uniprot.org/uniprot/AOC1_HUMAN AOC1_HUMAN] Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function.
== 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>
[[Category: Diamine oxidase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Guss, J M]]
[[Category: Guss JM]]
[[Category: McGrath, A P]]
[[Category: McGrath AP]]
[[Category: Aminoguanidine]]
[[Category: Cao]]
[[Category: Copper amine oxidase]]
[[Category: Dao]]
[[Category: Oxidoreductase]]
[[Category: Topaquinone]]
[[Category: Tpq]]
Retrieved from "https://proteopedia.org/3mph"