This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3a7d
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crystal Structures of rat Catechol-O-Methyltransferase complexed with new bi-substrate type inhibitor== | ==Crystal Structures of rat Catechol-O-Methyltransferase complexed with new bi-substrate type inhibitor== | ||
| - | <StructureSection load='3a7d' size='340' side='right' caption='[[3a7d]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='3a7d' size='340' side='right'caption='[[3a7d]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3a7d]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3a7d]] 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=3A7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A7D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FBN:5-DEOXY-5-[4-({[(2,3-DIHYDROXY-5-NITROPHENYL)CARBONYL]AMINO}METHYL)-1H-1,2,3-TRIAZOL-1-YL]ADENOSINE'>FBN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FBN:5-DEOXY-5-[4-({[(2,3-DIHYDROXY-5-NITROPHENYL)CARBONYL]AMINO}METHYL)-1H-1,2,3-TRIAZOL-1-YL]ADENOSINE'>FBN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vid|1vid]], [[1jr4|1jr4]], [[3a7e|3a7e]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vid|1vid]], [[1jr4|1jr4]], [[3a7e|3a7e]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Comt ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Comt ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7d OCA], [https://pdbe.org/3a7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a7d RCSB], [https://www.ebi.ac.uk/pdbsum/3a7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7d 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]] | ||
| Line 24: | Line 24: | ||
==See Also== | ==See Also== | ||
| - | *[[Catechol O-methyltransferase|Catechol O-methyltransferase]] | + | *[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Buffalo rat]] | [[Category: Buffalo rat]] | ||
[[Category: Catechol O-methyltransferase]] | [[Category: Catechol O-methyltransferase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Tsuji, E]] | [[Category: Tsuji, E]] | ||
[[Category: Alternative initiation]] | [[Category: Alternative initiation]] | ||
Revision as of 16:18, 22 December 2021
Crystal Structures of rat Catechol-O-Methyltransferase complexed with new bi-substrate type inhibitor
| |||||||||||
Categories: Buffalo rat | Catechol O-methyltransferase | Large Structures | Tsuji, E | Alternative initiation | Catecholamine metabolism | Cell membrane | Magnesium | Membrane | Metal-binding | Methyltransferase | Neurotransmitter degradation | Phosphoprotein | S-adenosyl-l-methionine | Signal-anchor | Transferase | Transmembrane
