2a14
From Proteopedia
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==Crystal Structure of Human Indolethylamine N-methyltransferase with SAH== | ==Crystal Structure of Human Indolethylamine N-methyltransferase with SAH== | ||
<StructureSection load='2a14' size='340' side='right' caption='[[2a14]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='2a14' size='340' side='right' caption='[[2a14]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Amine_N-methyltransferase Amine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.49 2.1.1.49] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Amine_N-methyltransferase Amine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.49 2.1.1.49] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a14 OCA], [http://pdbe.org/2a14 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a14 RCSB], [http://www.ebi.ac.uk/pdbsum/2a14 PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a14 OCA], [http://pdbe.org/2a14 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a14 RCSB], [http://www.ebi.ac.uk/pdbsum/2a14 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a14 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/2a14_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/2a14_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=2a14 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
== References == | == References == | ||
Revision as of 07:17, 9 May 2018
Crystal Structure of Human Indolethylamine N-methyltransferase with SAH
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Categories: Amine N-methyltransferase | Human | Arrowsmith, C H | Bochkarev, A | Dong, A | Edwards, A M | Loppnau, P | Plotnikov, A N | Structural genomic | Sundstrom, M | Wu, H | Zeng, H | Inmt | Sgc | Transferase
