1auk Summary

pdbe.org/1auk
spacer

HUMAN ARYLSULFATASE A

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 100% 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
A ARYLSULFATASE A P15289 (19-507) (ARSA_HUMAN)search Homo sapienssearch 100% 489 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P15289 (19 - 507) ARYLSULFATASE A Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P15289) Arylsulfatasesearch Alkaline Phosphatase, subunit Asearch, Arylsulfatase, C-terminal domainsearch PF00884: Sulfatasesearch, PF14707: C-terminal region of aryl-sulfatasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P15289) sulfuric ester hydrolase activitysearch calcium ion bindingsearch arylsulfatase activitysearch metal ion bindingsearch cerebroside-sulfatase activitysearch hydrolase activitysearch catalytic activitysearch sphingolipid metabolic processsearch binding of sperm to zona pellucidasearch response to methylmercurysearch response to ethanolsearch response to estrogensearch post-translational protein modificationsearch central nervous system developmentsearch cellular protein metabolic processsearch small molecule metabolic processsearch autophagysearch response to pHsearch glycosphingolipid metabolic processsearch response to nutrientsearch metabolic processsearch lysosomesearch acrosomal vesiclesearch endosomesearch extracellular vesicular exosomesearch lysosomal lumensearch endoplasmic reticulum lumensearch extracellular spacesearch cytoplasmsearch plasma membranesearch extrinsic component of external side of plasma membranesearch integral component of membranesearch

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