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2a14

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<StructureSection load='2a14' size='340' side='right'caption='[[2a14]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2a14' size='340' side='right'caption='[[2a14]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2a14]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A14 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2a14]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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>
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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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<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>
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<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>
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<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>
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<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 ==
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[[http://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>
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[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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Amine N-methyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bochkarev, A]]
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[[Category: Bochkarev A]]
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[[Category: Dong, A]]
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[[Category: Dong A]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Loppnau, P]]
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[[Category: Loppnau P]]
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[[Category: Plotnikov, A N]]
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[[Category: Plotnikov AN]]
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[[Category: Structural genomic]]
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[[Category: Sundstrom M]]
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[[Category: Sundstrom, M]]
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[[Category: Wu H]]
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[[Category: Wu, H]]
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[[Category: Zeng H]]
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[[Category: Zeng, H]]
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[[Category: Inmt]]
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[[Category: Sgc]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of Human Indolethylamine N-methyltransferase with SAH

PDB ID 2a14

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