5lsa: Difference between revisions
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==human catechol O-methyltransferase in complex with SAM and DNC at 1.50A== | ==human catechol O-methyltransferase in complex with SAM and DNC at 1.50A== | ||
<StructureSection load='5lsa' size='340' side='right' caption='[[5lsa]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='5lsa' size='340' side='right'caption='[[5lsa]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lsa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LSA OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5lsa]] is a 1 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=5LSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LSA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lsa OCA], [https://pdbe.org/5lsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lsa RCSB], [https://www.ebi.ac.uk/pdbsum/5lsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lsa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/COMT_HUMAN COMT_HUMAN] 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ehler A]] | ||
[[Category: | [[Category: Lerner C]] | ||
[[Category: | [[Category: Rudolph MG]] | ||
Latest revision as of 21:44, 18 October 2023
human catechol O-methyltransferase in complex with SAM and DNC at 1.50Ahuman catechol O-methyltransferase in complex with SAM and DNC at 1.50A
Structural highlights
FunctionCOMT_HUMAN 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 |
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