1efh: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=A3P:ADENOSINE-3'-5'-DIPHOSPHATE'>A3P</scene> | |LIGAND= <scene name='pdbligand=A3P:ADENOSINE-3'-5'-DIPHOSPHATE'>A3P</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= CDNA LIBRARY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CDNA LIBRARY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1efh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efh OCA], [http://www.ebi.ac.uk/pdbsum/1efh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1efh RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Pedersen, L C.]] | [[Category: Pedersen, L C.]] | ||
[[Category: Petrotchenko, E V.]] | [[Category: Petrotchenko, E V.]] | ||
[[Category: a3p]] | [[Category: a3p]] | ||
[[Category: dhea]] | [[Category: dhea]] | ||
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[[Category: sult2a3]] | [[Category: sult2a3]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:26 2008'' | ||
