1fsu

Revision as of 21:14, 29 October 2007 by OCA (talk | contribs) (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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4-SULFATASE (HUMAN)

File:1fsu.gif


1fsu, resolution 2.5Å

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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 [[1]], with EC number [3.1.6.12]. 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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