1cjm: Difference between revisions
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'''HUMAN SULT1A3 WITH SULFATE BOUND''' | {{Structure | ||
|PDB= 1cjm |SIZE=350|CAPTION= <scene name='initialview01'>1cjm</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HUMAN SULT1A3 WITH SULFATE BOUND''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CJM is a [ | 1CJM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJM OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of human catecholamine sulfotransferase., Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL, J Mol Biol. 1999 Oct 29;293(3):521-30. PMID:[http:// | Crystal structure of human catecholamine sulfotransferase., Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL, J Mol Biol. 1999 Oct 29;293(3):521-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10543947 10543947] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hast3]] | [[Category: hast3]] | ||
[[Category: pap]] | [[Category: pap]] | ||
[[Category: | [[Category: pap]] | ||
[[Category: sulfotransferase]] | [[Category: sulfotransferase]] | ||
[[Category: sult1a3]] | [[Category: sult1a3]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:25:20 2008'' | ||
Revision as of 11:25, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN SULT1A3 WITH SULFATE BOUND
OverviewOverview
Sulfonation, like phosphorylation, can modify the activity of a variety of biological molecules. The sulfotransferase enzymes sulfonate neurotransmitters, drugs, steroid hormones, dietary carcinogens and proteins. SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. The crystal structure of SULT1A3 with a sulfate bound at the active site, has been determined at 2.4 A resolution. Although the core alpha/beta fold is like that of estrogen and heparan sulfotransferases, major differences occur in and around the active site. Most notably, several regions surrounding the active site, including a section of 40 residues, are disordered in SULT1A3. Regions that are topologically equivalent to the disordered parts of SULT1A3 are involved in substrate and cofactor binding in estrogen and heparan sulfotransferase. Flexibility in these regions suggests that ligand binding elicits a disorder-order transition in and around the active site of sulfotransferases and might contribute to the broad substrate specificity of these enzymes.
DiseaseDisease
Known diseases associated with this structure: Alzheimer disease-4 OMIM:[600759], Cardiomyopathy, dilated, 1V OMIM:[600759]
About this StructureAbout this Structure
1CJM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human catecholamine sulfotransferase., Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL, J Mol Biol. 1999 Oct 29;293(3):521-30. PMID:10543947
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