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3cuk

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==Crystal structure of human D-amino acid oxidase: bound to an inhibitor==
==Crystal structure of human D-amino acid oxidase: bound to an inhibitor==
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<StructureSection load='3cuk' size='340' side='right' caption='[[3cuk]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
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<StructureSection load='3cuk' size='340' side='right'caption='[[3cuk]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3cuk]] is a 4 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=3CUK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CUK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3cuk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CUK 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=4P5:4H-FURO[3,2-B]PYRROLE-5-CARBOXYLIC+ACID'>4P5</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4P5:4H-FURO[3,2-B]PYRROLE-5-CARBOXYLIC+ACID'>4P5</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAO, DAMOX ([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">DAO, DAMOX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </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=3cuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cuk OCA], [http://pdbe.org/3cuk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cuk RCSB], [http://www.ebi.ac.uk/pdbsum/3cuk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cuk ProSAT]</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=3cuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cuk OCA], [https://pdbe.org/3cuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cuk RCSB], [https://www.ebi.ac.uk/pdbsum/3cuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cuk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/OXDA_HUMAN OXDA_HUMAN]] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.<ref>PMID:17303072</ref>
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[[https://www.uniprot.org/uniprot/OXDA_HUMAN OXDA_HUMAN]] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.<ref>PMID:17303072</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Amino acid oxidase|Amino acid oxidase]]
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*[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: D-amino-acid oxidase]]
[[Category: D-amino-acid oxidase]]
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Munshi, S]]
[[Category: Munshi, S]]
[[Category: Prasad, S]]
[[Category: Prasad, S]]

Revision as of 07:45, 2 February 2022

Crystal structure of human D-amino acid oxidase: bound to an inhibitor

PDB ID 3cuk

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