1efh | pdb_00001efh

CRYSTAL STRUCTURE OF THE HUMAN HYDROXYSTEROID SULFOTRANSFERASE IN THE PRESENCE OF PAP

spinqualitylabelsall models 1efh, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1efh is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: A3P Gene: CDNA LIBRARY (HUMAN) Activity: Alcohol sulfotransferase, with EC number 2.8.2.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sulfotransferase

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