1auk Summary



The structure was published by Lukatela, G., Krauss, N., Theis, K., et al., Gieselmann, V., von Figura, K., and Saenger, W., in 1998 in a paper entitled "Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1997.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of ARYLSULFATASE A. This molecule has the UniProt identifier P15289 (ARSA_HUMAN)search. The sample contained 489 residues which is < 90% of the natural sequence. Out of 489 residues 478 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homooctamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
Homo sapienssearch Not available 489 98%

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A () catalytic activitysearch sulfuric ester hydrolase activitysearch calcium ion bindingsearch hydrolase activitysearch cerebroside-sulfatase activitysearch metal ion bindingsearch arylsulfatase activitysearch metabolic processsearch autophagysearch binding of sperm to zona pellucidasearch sphingolipid metabolic processsearch response to estrogensearch small molecule metabolic processsearch cellular protein metabolic processsearch response to ethanolsearch response to pHsearch post-translational protein modificationsearch central nervous system developmentsearch response to methylmercurysearch response to nutrientsearch glycosphingolipid metabolic processsearch lysosomesearch cytoplasmsearch endoplasmic reticulum lumensearch extrinsic component of external side of plasma membranesearch plasma membranesearch lysosomal lumensearch extracellular spacesearch acrosomal vesiclesearch integral component of membranesearch endosomesearch extracellular vesicular exosomesearch

Chain InterPro annotation
A Sulfatasesearch Alkaline phosphatase-like, alpha/beta/alphasearch Alkaline-phosphatase-like, core domainsearch Sulfatase, conserved sitesearch