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5lqa
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5lqa is ON HOLD Authors: Ehler, A., Ellermann, M., Rudolph, M.G. Description: rat catechol O-methyltransferase at high pH in complex with a bisubst...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==rat catechol O-methyltransferase at high pH in complex with a bisubstrate inhibitor== | |
| + | <StructureSection load='5lqa' size='340' side='right'caption='[[5lqa]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lqa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LQA 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]] 1.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=619:N-[(E)-3-[(2R,3S,4R,5R)-5-(6-ETHYLAMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]PROP-2-ENYL]-5-(4-FLUOROPHENYL)-2,3-DIHYDROXY-BENZAMIDE'>619</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lqa OCA], [https://pdbe.org/5lqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lqa RCSB], [https://www.ebi.ac.uk/pdbsum/5lqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lqa ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/COMT_RAT COMT_RAT] Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. | ||
| - | + | ==See Also== | |
| - | + | *[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Ehler | + | [[Category: Large Structures]] |
| - | [[Category: Ellermann | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Rudolph | + | [[Category: Ehler A]] |
| + | [[Category: Ellermann M]] | ||
| + | [[Category: Rudolph MG]] | ||
Current revision
rat catechol O-methyltransferase at high pH in complex with a bisubstrate inhibitor
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