1XC6
Native Structure Of Beta-Galactosidase from Penicillium sp. in complex with Galactose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004565 | molecular_function | beta-galactosidase activity |
| A | 0005534 | molecular_function | galactose binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005990 | biological_process | lactose catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PROSITE/UniProt
| site_id | PS01182 |
| Number of Residues | 13 |
| Details | GLYCOSYL_HYDROL_F35 Glycosyl hydrolases family 35 putative active site. GGPIIlyQpENEY |
| Chain | Residue | Details |
| A | GLY189-TYR201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15491613","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XC6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15491613","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XC6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
