1fsu: Difference between revisions
New page: left|200px<br /> <applet load="1fsu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fsu, resolution 2.5Å" /> '''4-SULFATASE (HUMAN)'... |
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==About this Structure== | ==About this Structure== | ||
1FSU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA and CL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.6.12 3.1.6.12]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FSU OCA]]. | 1FSU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA and CL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/N-acetylgalactosamine-4-sulfatase N-acetylgalactosamine-4-sulfatase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.6.12 3.1.6.12]]. Structure known Active Sites: MEB and SAL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FSU OCA]]. | ||
==Reference== | ==Reference== | ||
Structure of a human lysosomal sulfatase., Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM, Structure. 1997 Feb 15;5(2):277-89. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9032078 9032078] | Structure of a human lysosomal sulfatase., Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM, Structure. 1997 Feb 15;5(2):277-89. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9032078 9032078] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: N-acetylgalactosamine-4-sulfatase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bond, C.]] | [[Category: Bond, C.]] | ||
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[[Category: sulfatase]] | [[Category: sulfatase]] | ||
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Revision as of 14:08, 30 October 2007
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4-SULFATASE (HUMAN)
OverviewOverview
BACKGROUND:. Sulfatases catalyze the hydrolysis of sulfuric acid esters, from a wide variety of substrates including glycosaminoglycans, glycolipids and steroids. There is sufficient common sequence similarity, within the class of sulfatase enzymes to indicate that they have a common, structure. Deficiencies of specific lysosomal sulfatases that are involved, in the degradation of glycosamino-glycans lead to rare inherited clinical, disorders termed mucopolysaccharidoses. In sufferers of multiple sulfatase, deficiency, all sulfatases are inactive because an essential, post-translational modification of a specific active-site cysteine residue, to oxo-alanine does not occur. Studies of this disorder have contributed, to location and characterization of the sulfatase active site. To, ... [(full description)]
About this StructureAbout this Structure
1FSU is a [Single protein] structure of sequence from [Homo sapiens] with CA and CL as [ligands]. Active as [N-acetylgalactosamine-4-sulfatase], with EC number [3.1.6.12]. Structure known Active Sites: MEB and SAL. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of a human lysosomal sulfatase., Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM, Structure. 1997 Feb 15;5(2):277-89. PMID:9032078
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