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4yjh
From Proteopedia
(Difference between revisions)
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==Crystal structure of DAAO(Y228L/R283G) variant (R-2-phenylpyrrolidine binding form)== | ==Crystal structure of DAAO(Y228L/R283G) variant (R-2-phenylpyrrolidine binding form)== | ||
| - | <StructureSection load='4yjh' size='340' side='right' caption='[[4yjh]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4yjh' size='340' side='right'caption='[[4yjh]], [[Resolution|resolution]] 2.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4yjh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YJH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yjh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YJH FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=96B:(2R)-2-PHENYLPYRROLIDINE'>96B</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=96B:(2R)-2-PHENYLPYRROLIDINE'>96B</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yjg|4yjg]], [[4yjf|4yjf]], [[4yjd|4yjd]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yjg|4yjg]], [[4yjf|4yjf]], [[4yjd|4yjd]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr> | ||
<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> | <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> | ||
| - | <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=4yjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yjh OCA], [http://pdbe.org/4yjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yjh RCSB], [http://www.ebi.ac.uk/pdbsum/4yjh PDBsum]</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=4yjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yjh OCA], [http://pdbe.org/4yjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yjh RCSB], [http://www.ebi.ac.uk/pdbsum/4yjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yjh ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/OXDA_PIG OXDA_PIG]] 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. | [[http://www.uniprot.org/uniprot/OXDA_PIG OXDA_PIG]] 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. | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: D-amino-acid oxidase]] | [[Category: D-amino-acid oxidase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pig]] | ||
[[Category: Asano, Y]] | [[Category: Asano, Y]] | ||
[[Category: Ishitsubo, E]] | [[Category: Ishitsubo, E]] | ||
Revision as of 07:24, 12 June 2019
Crystal structure of DAAO(Y228L/R283G) variant (R-2-phenylpyrrolidine binding form)
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