Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003943 | molecular_function | N-acetylgalactosamine-4-sulfatase activity |
| A | 0004065 | molecular_function | arylsulfatase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005764 | cellular_component | lysosome |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0006914 | biological_process | autophagy |
| A | 0007040 | biological_process | lysosome organization |
| A | 0007041 | biological_process | lysosomal transport |
| A | 0007584 | biological_process | response to nutrient |
| A | 0008484 | molecular_function | sulfuric ester hydrolase activity |
| A | 0009268 | biological_process | response to pH |
| A | 0009986 | cellular_component | cell surface |
| A | 0010632 | biological_process | regulation of epithelial cell migration |
| A | 0010976 | biological_process | positive regulation of neuron projection development |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0035578 | cellular_component | azurophil granule lumen |
| A | 0043202 | cellular_component | lysosomal lumen |
| A | 0043627 | biological_process | response to estrogen |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051597 | biological_process | response to methylmercury |
| A | 0061580 | biological_process | colon epithelial cell migration |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | MEB |
| Number of Residues | 5 |
| Details | THIS IS THE METAL BINDING SITE. THE METAL WAS IDENTIFIED AS CALCIUM BY ITS PEAK HEIGHT IN DIFFERENCE ELECTRON DENSITY MAPS, BY SUCCESSIVE TEMPERATURE FACTOR REFINEMENT AND BY THE NATURE AND GEOMETRY OF THE COORDINATING LIGANDS. |
| Chain | Residue |
| A | ASP53 |
| A | ASP54 |
| A | ALS91 |
| A | ASP300 |
| A | ASN301 |
| site_id | SAL |
| Number of Residues | 6 |
| Details | THESE RESIDUES AND THE METAL ION STABILIZE THE SULFATE ESTER RESIDUE 91. TOGETHER WITH THE METAL BINDING SITE THIS FORMS THE CENTER OF THE CATALYTIC ACTIVE SITE. |
| Chain | Residue |
| A | ARG95 |
| A | HIS147 |
| A | ALS91 |
| A | HIS242 |
| A | LYS318 |
| A | LYS145 |
Functional Information from PROSITE/UniProt
| site_id | PS00149 |
| Number of Residues | 11 |
| Details | SULFATASE_2 Sulfatases signature 2. GYtThmVGK.WH |
| Chain | Residue | Details |
| A | GLY137-HIS147 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ALS91 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | HIS147 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP53 | |
| A | ASP54 | |
| A | ASP300 | |
| A | ASN301 | |
| Chain | Residue | Details |
| A | ALS91 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS145 | |
| A | HIS242 | |
| A | LYS318 | |
| Chain | Residue | Details |
| A | ALS91 | |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN188 | |
| A | ASN458 | |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
| Chain | Residue | Details |
| A | ASN279 | |
| A | ASN426 | |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305 |
| Chain | Residue | Details |
| A | ASN291 | |
| Chain | Residue | Details |
| A | ASN366 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1hdh |
| Chain | Residue | Details |
| A | HIS242 | |
| A | LYS145 | |
| A | ARG95 | |
| A | ASP300 | |
| A | LYS318 | |
| A | HIS147 | |
