2e48

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2e48]] 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E48 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2e48]] 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=2E48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E48 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2du8|2du8]], [[2e49|2e49]], [[2e4a|2e4a]], [[2e82|2e82]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2du8|2du8]], [[2e49|2e49]], [[2e4a|2e4a]], [[2e82|2e82]]</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/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'>[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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [http://www.ebi.ac.uk/pdbsum/2e48 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=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB], [http://www.ebi.ac.uk/pdbsum/2e48 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/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==
*[[Amino acid oxidase|Amino acid oxidase]]
*[[Amino acid oxidase|Amino acid oxidase]]
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*[[Rossmann fold|Rossmann fold]]
== References ==
== References ==
<references/>
<references/>
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[[Category: D-amino-acid oxidase]]
[[Category: D-amino-acid oxidase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Fukui, K.]]
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[[Category: Fukui, K]]
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[[Category: Imagawa, T.]]
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[[Category: Imagawa, T]]
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[[Category: Kawazoe, T.]]
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[[Category: Kawazoe, T]]
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[[Category: Tsuge, H.]]
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[[Category: Tsuge, H]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Structurally ambivalent peptide]]
[[Category: Structurally ambivalent peptide]]
[[Category: Substrate-free holoenzyme]]
[[Category: Substrate-free holoenzyme]]

Revision as of 07:52, 25 December 2014

Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme

2e48, resolution 2.90Å

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