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). 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):