3mph

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== 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 [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>
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</td></tr><tr><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><br>
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</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>
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<tr><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>
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<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>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hi7|3hi7]], [[3hig|3hig]], [[3hii|3hii]], [[3k5t|3k5t]]</td></tr>
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<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>
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<tr><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>
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<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>
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<tr><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>
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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/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>
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<tr><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://www.rcsb.org/pdb/explore.do?structureId=3mph RCSB], [http://www.ebi.ac.uk/pdbsum/3mph 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=3mph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mph OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mph RCSB], [http://www.ebi.ac.uk/pdbsum/3mph PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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Correlation of Active Site Metal Content in Human Diamine Oxidase with Trihydroxyphenylalanine Quinone Cofactor Biogenesis .,McGrath AP, Caradoc-Davies T, Collyer CA, Guss JM Biochemistry. 2010 Sep 1. PMID:20722416<ref>PMID:20722416</ref>
Correlation of Active Site Metal Content in Human Diamine Oxidase with Trihydroxyphenylalanine Quinone Cofactor Biogenesis .,McGrath AP, Caradoc-Davies T, Collyer CA, Guss JM Biochemistry. 2010 Sep 1. PMID:20722416<ref>PMID:20722416</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
== References ==
== References ==
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[[Category: Diamine oxidase]]
[[Category: Diamine oxidase]]
[[Category: Human]]
[[Category: Human]]
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[[Category: Guss, J M.]]
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[[Category: Guss, J M]]
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[[Category: McGrath, A P.]]
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[[Category: McGrath, A P]]
[[Category: Aminoguanidine]]
[[Category: Aminoguanidine]]
[[Category: Cao]]
[[Category: Cao]]
[[Category: Copper amine oxidase]]
[[Category: Copper amine oxidase]]
[[Category: Dao]]
[[Category: Dao]]
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[[Category: Diamine oxidase]]
 
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[[Category: Human]]
 
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Topaquinone]]
[[Category: Topaquinone]]
[[Category: Tpq]]
[[Category: Tpq]]

Revision as of 22:19, 25 December 2014

The structure of human diamine oxidase complexed with an inhibitor aminoguanidine

3mph, resolution 2.05Å

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OCA

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