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4pyo
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Humanized rat COMT bound to SAH, semi-holo form== |
| - | + | <StructureSection load='4pyo' size='340' side='right' caption='[[4pyo]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4pyo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PYO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PYO FirstGlance]. <br> | |
| - | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene><br> | |
| - | + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p7k|4p7k]], [[4p7f|4p7f]], [[4p7g|4p7g]], [[4p7j|4p7j]], [[4pyj|4pyj]], [[4pyk|4pyk]], [[4pyl|4pyl]], [[4pym|4pym]], [[4pyn|4pyn]], [[4pyq|4pyq]], [[4pyi|4pyi]]</td></tr> | |
| - | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] </span></td></tr> | |
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pyo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pyo RCSB], [http://www.ebi.ac.uk/pdbsum/4pyo PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Catechol O-methyltransferase]] | ||
| + | [[Category: Benz, J.]] | ||
| + | [[Category: Ehler, A.]] | ||
| + | [[Category: Rudolph, M G.]] | ||
| + | [[Category: Schlatter, D.]] | ||
| + | [[Category: Alternative initiation]] | ||
| + | [[Category: Catecholamine metabolism]] | ||
| + | [[Category: Cell membrane]] | ||
| + | [[Category: Conformational change]] | ||
| + | [[Category: Enzyme mechanism]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Methyltransferase]] | ||
| + | [[Category: Neurotransmitter degradation]] | ||
| + | [[Category: Phosphoprotein]] | ||
| + | [[Category: Signal-anchor]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Transmembrane anchor]] | ||
Revision as of 08:58, 11 June 2014
Humanized rat COMT bound to SAH, semi-holo form
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Categories: Catechol O-methyltransferase | Benz, J. | Ehler, A. | Rudolph, M G. | Schlatter, D. | Alternative initiation | Catecholamine metabolism | Cell membrane | Conformational change | Enzyme mechanism | Membrane | Metal-binding | Methyltransferase | Neurotransmitter degradation | Phosphoprotein | Signal-anchor | Transferase | Transmembrane anchor
