1EUT
SIALIDASE, LARGE 68KD FORM, COMPLEXED WITH GALACTOSE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004308 | molecular_function | exo-alpha-sialidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006689 | biological_process | ganglioside catabolic process |
| A | 0009313 | biological_process | oligosaccharide catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1 |
| Chain | Residue |
| A | ASN528 |
| A | ASP531 |
| A | ASN533 |
| A | THR536 |
| A | ALA639 |
| A | GLU640 |
| site_id | ACT |
| Number of Residues | 9 |
| Details | ACTIVE SITE. SITE INCLUDES TWO CONTACTS WITH SYMMETRY-RELATED MOLECULES. |
| Chain | Residue |
| A | GLN224 |
| A | GLY245 |
| A | ALA250 |
| A | GLY292 |
| A | ASN311 |
| A | PHE318 |
| A | ALA619 |
| A | TYR635 |
| A | ALA637 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 11 |
| Details | Repeat: {"description":"BNR 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Repeat: {"description":"BNR 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | Repeat: {"description":"BNR 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 11 |
| Details | Repeat: {"description":"BNR 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 11 |
| Details | Repeat: {"description":"BNR 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 150 |
| Details | Domain: {"description":"F5/8 type C","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1euu |
| Chain | Residue | Details |
| A | ASP92 | |
| A | TYR370 | |
| A | GLU260 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 835 |
| Chain | Residue | Details |
| A | ASP92 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| A | GLU260 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| A | TYR370 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
