1zd1

<table><tr><td colspan='2'>[[1zd1]] is a 2 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=1ZD1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ZD1 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SULT4A1, SULTX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1zd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd1 OCA], [http://pdbe.org/1zd1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zd1 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zd1 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/ST4A1_HUMAN ST4A1_HUMAN]] Atypical sulfotransferase family member with very low affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in the metabolism of drugs and neurotransmitters in the CNS.<ref>PMID:17425406</ref>

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== Publication Abstract from PubMed ==

The human cytosolic sulfotransfases (hSULTs) comprise a family of 12 phase II enzymes involved in the metabolism of drugs and hormones, the bioactivation of carcinogens, and the detoxification of xenobiotics. Knowledge of the structural and mechanistic basis of substrate specificity and activity is crucial for understanding steroid and hormone metabolism, drug sensitivity, pharmacogenomics, and response to environmental toxins. We have determined the crystal structures of five hSULTs for which structural information was lacking, and screened nine of the 12 hSULTs for binding and activity toward a panel of potential substrates and inhibitors, revealing unique "chemical fingerprints" for each protein. The family-wide analysis of the screening and structural data provides a comprehensive, high-level view of the determinants of substrate binding, the mechanisms of inhibition by substrates and environmental toxins, and the functions of the orphan family members SULT1C3 and SULT4A1. Evidence is provided for structural "priming" of the enzyme active site by cofactor binding, which influences the spectrum of small molecules that can bind to each enzyme. The data help explain substrate promiscuity in this family and, at the same time, reveal new similarities between hSULT family members that were previously unrecognized by sequence or structure comparison alone.

Structural and chemical profiling of the human cytosolic sulfotransferases.,Allali-Hassani A, Pan PW, Dombrovski L, Najmanovich R, Tempel W, Dong A, Loppnau P, Martin F, Thornton J, Edwards AM, Bochkarev A, Plotnikov AN, Vedadi M, Arrowsmith CH PLoS Biol. 2007 May;5(5):e97. PMID:17425406<ref>PMID:17425406</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1zd1" style="background-color:#fffaf0;"></div>

*[[Sulfotransferase|Sulfotransferase]]

[[Category: Human]]

[[Category: Arrowsmith, C H]]

[[Category: Bochkarev, A]]

[[Category: Dombrovski, L]]

[[Category: Dong, A]]

[[Category: Edwards, A M]]

[[Category: Loppnau, P]]

[[Category: Plotnikov, A N]]

[[Category: Structural genomic]]

[[Category: Sundstrom, M]]

[[Category: Transferase]]