1efh

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

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene></td></tr>

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

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_sulfotransferase Alcohol sulfotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.2 2.8.2.2] </span></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=1efh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efh OCA], [http://pdbe.org/1efh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1efh RCSB], [http://www.ebi.ac.uk/pdbsum/1efh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1efh ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/ST2A1_HUMAN ST2A1_HUMAN]] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands.

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== Publication Abstract from PubMed ==

The crystal structure of SULT2A3 human hydroxysteroid sulfotransferase has been solved at 2.4 A resolution in the presence of 3'-phosphoadenosine 5'-phosphate (PAP). The overall structure is similar to those of SULT1 enzymes such as estrogen sulfotransferase and the PAP binding site is conserved, however, significant differences exist in the positions of loops Pro14-Ser20, Glu79-Ile82 and Tyr234-Gln244 in the substrate binding pocket. Moreover, protein interaction in the crystal structure has revealed a possible dimer-directed conformational alteration that may regulate the SULT activity.

Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase.,Pedersen LC, Petrotchenko EV, Negishi M FEBS Lett. 2000 Jun 9;475(1):61-4. PMID:10854859<ref>PMID:10854859</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 1efh" style="background-color:#fffaf0;"></div>

*[[Sulfotransferase|Sulfotransferase]]

[[Category: Alcohol sulfotransferase]]

[[Category: Human]]

[[Category: Negishi, M]]

[[Category: Pedersen, L C]]

[[Category: Petrotchenko, E V]]

[[Category: Transferase]]