2a14
From Proteopedia
(Difference between revisions)
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<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=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2a14]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2a14]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A14 FirstGlance]. <br> |
| - | </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" id="ligandDat"><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'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Amine_N-methyltransferase Amine N-methyltransferase], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a14 OCA], [https://pdbe.org/2a14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a14 RCSB], [https://www.ebi.ac.uk/pdbsum/2a14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a14 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/INMT_HUMAN INMT_HUMAN]] Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds (By similarity). Catalyzes the N-methylation of tryptamine and structurally related compounds.<ref>PMID:10552930</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 14:34, 17 November 2021
Crystal Structure of Human Indolethylamine N-methyltransferase with SAH
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Categories: Amine N-methyltransferase | Human | Large Structures | 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
