4pyj: Difference between revisions
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==human apo-COMT, single domain swap== | ==human apo-COMT, single domain swap== | ||
<StructureSection load='4pyj' size='340' side='right' caption='[[4pyj]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4pyj' size='340' side='right'caption='[[4pyj]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pyj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PYJ OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4pyj]] 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=4PYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PYJ FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4pyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pyj OCA], [https://pdbe.org/4pyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pyj RCSB], [https://www.ebi.ac.uk/pdbsum/4pyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pyj ProSAT]</span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<table> | == 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: Benz | [[Category: Large Structures]] | ||
[[Category: Ehler | [[Category: Benz J]] | ||
[[Category: Rudolph | [[Category: Ehler A]] | ||
[[Category: Schlatter | [[Category: Rudolph MG]] | ||
[[Category: Schlatter D]] | |||
Latest revision as of 15:43, 1 March 2024
human apo-COMT, single domain swaphuman apo-COMT, single domain swap
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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