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3hvk
From Proteopedia
(Difference between revisions)
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<StructureSection load='3hvk' size='340' side='right'caption='[[3hvk]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='3hvk' size='340' side='right'caption='[[3hvk]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3hvk]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3hvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HVK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=719:N-[(E)-3-[(2R,3S,4R,5R)-3,4-DIHYDROXY-5-[6-(2-HYDROXYETHYLAMINO)PURIN-9-YL]OXOLAN-2-YL]PROP-2-ENYL]-5-(4-FLUOROPHENYL)-2,3-DIHYDROXY-BENZAMIDE'>719</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></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=719:N-[(E)-3-[(2R,3S,4R,5R)-3,4-DIHYDROXY-5-[6-(2-HYDROXYETHYLAMINO)PURIN-9-YL]OXOLAN-2-YL]PROP-2-ENYL]-5-(4-FLUOROPHENYL)-2,3-DIHYDROXY-BENZAMIDE'>719</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></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hvh|3hvh]], [[3hvi|3hvi]], [[3hvj|3hvj]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hvh|3hvh]], [[3hvi|3hvi]], [[3hvj|3hvj]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] </span></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=3hvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hvk OCA], [https://pdbe.org/3hvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hvk RCSB], [https://www.ebi.ac.uk/pdbsum/3hvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hvk ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 11:58, 30 March 2022
Rat catechol O-methyltransferase in complex with a catechol-type, purine-containing bisubstrate inhibitor - humanized form
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Categories: Buffalo rat | Catechol O-methyltransferase | Large Structures | Benz, J | Ehler, A | Rudolph, M G | Schlatter, D | Stihle, M | Alternative initiation | Catecholamine metabolism | Cell membrane | Magnesium | Membrane | Metal-binding | Methyltransferase | Neurotransmitter degradation | Phosphoprotein | S-adenosyl-l-methionine | Signal-anchor | Transferase | Transmembrane
