8hy5: Difference between revisions
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New page: '''Unreleased structure''' The entry 8hy5 is ON HOLD Authors: Khan, S., Upadhyay, S., Kumar, A., Dave, U., Gomes, J. Description: Structure of D-amino acid oxidase mutant R38H [[Catego... |
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==Structure of D-amino acid oxidase mutant R38H== | |||
<StructureSection load='8hy5' size='340' side='right'caption='[[8hy5]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8hy5]] 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=8HY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HY5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8hy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hy5 OCA], [https://pdbe.org/8hy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hy5 RCSB], [https://www.ebi.ac.uk/pdbsum/8hy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hy5 ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: | == Function == | ||
[[Category: Khan | [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> | ||
[[Category: Kumar | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Dave U]] | |||
[[Category: Gomes J]] | |||
[[Category: Khan S]] | |||
[[Category: Kumar A]] | |||
[[Category: Upadhyay S]] | |||
Latest revision as of 12:24, 10 January 2024
Structure of D-amino acid oxidase mutant R38H
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