3a7d: Difference between revisions

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New page: '''Unreleased structure''' The entry 3a7d is ON HOLD until Paper Publication Authors: Tsuji, E. Description: Crystal Structures of rat Catechol-O-Methyltransferase complexed with new b...
 
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'''Unreleased structure'''


The entry 3a7d is ON HOLD  until Paper Publication
==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]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3a7d]] 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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='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>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/3a7d_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a7d ConSurf].
<div style="clear:both"></div>


Authors: Tsuji, E.
==See Also==
 
*[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]]
Description: Crystal Structures of rat Catechol-O-Methyltransferase complexed with new bi-substrate type inhibitor
__TOC__
 
</StructureSection>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct  7 13:39:45 2009''
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Tsuji E]]