1KTB
The Structure of alpha-N-Acetylgalactosaminidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004557 | molecular_function | alpha-galactosidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005764 | cellular_component | lysosome |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008456 | molecular_function | alpha-N-acetylgalactosaminidase activity |
| A | 0009311 | biological_process | oligosaccharide metabolic process |
| A | 0016139 | biological_process | glycoside catabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PROSITE/UniProt
| site_id | PS00512 |
| Number of Residues | 17 |
| Details | ALPHA_GALACTOSIDASE Alpha-galactosidase signature. GYkyInIDDc.Waakq...RD |
| Chain | Residue | Details |
| A | GLY54-ASP70 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | ASP140 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | ASP201 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP201 | |
| A | ASP61 | |
| A | LYS138 | |
| A | SER172 | |
| A | ARG197 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12005440 |
| Chain | Residue | Details |
| A | ASN161 | |
| A | ASN185 | |
| A | ASN369 |
