3u3k

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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=3u3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u3k RCSB], [http://www.ebi.ac.uk/pdbsum/3u3k 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=3u3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u3k RCSB], [http://www.ebi.ac.uk/pdbsum/3u3k PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/ST1A1_HUMAN ST1A1_HUMAN]] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.<ref>PMID:12471039</ref> <ref>PMID:16221673</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 21:50, 25 December 2014

Crystal structure of hSULT1A1 bound to PAP and 2-Naphtol

3u3k, resolution 2.36Å

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