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2zlb
From Proteopedia
(Difference between revisions)
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==Crystal structure of APO form of rat catechol-O-methyltransferase== | ==Crystal structure of APO form of rat catechol-O-methyltransferase== | ||
| - | <StructureSection load='2zlb' size='340' side='right' caption='[[2zlb]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='2zlb' size='340' side='right'caption='[[2zlb]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2zlb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZLB OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[2zlb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZLB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZLB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=SO4:SULFATE+ION'>SO4</scene></td></tr> |
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vid|1vid]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vid|1vid]]</td></tr> | ||
<tr id='activity'><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 id='activity'><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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zlb OCA], [http://pdbe.org/2zlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zlb RCSB], [http://www.ebi.ac.uk/pdbsum/2zlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zlb ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
| - | *[[Catechol O-methyltransferase|Catechol O-methyltransferase]] | + | *[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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[[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 12:06, 29 July 2020
Crystal structure of APO form of rat catechol-O-methyltransferase
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Categories: Buffalo rat | Catechol O-methyltransferase | Large Structures | Tsuji, E | Alternative initiation | Catecholamine metabolism | Cytoplasm | Magnesium | Membrane | Metal-binding | Methyltransferase | Neurotransmitter degradation | Phosphoprotein | S-adenosyl-l-methionine | Signal-anchor | Transferase | Transmembrane

