1Q4N
Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0003824 | molecular_function | catalytic activity |
| X | 0004556 | molecular_function | alpha-amylase activity |
| X | 0005509 | molecular_function | calcium ion binding |
| X | 0005576 | cellular_component | extracellular region |
| X | 0005615 | cellular_component | extracellular space |
| X | 0005975 | biological_process | carbohydrate metabolic process |
| X | 0009311 | biological_process | oligosaccharide metabolic process |
| X | 0016787 | molecular_function | hydrolase activity |
| X | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| X | 0031404 | molecular_function | chloride ion binding |
| X | 0043169 | molecular_function | cation binding |
| X | 0046872 | molecular_function | metal ion binding |
| X | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA X 950 |
| Chain | Residue |
| X | ASN100 |
| X | ARG158 |
| X | ASP167 |
| X | HIS201 |
| X | HOH526 |
| X | HOH563 |
| X | HOH587 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL X 951 |
| Chain | Residue |
| X | ARG337 |
| X | ARG195 |
| X | ASN298 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TAM X 900 |
| Chain | Residue |
| X | TYR62 |
| X | HIS101 |
| X | ASP197 |
| X | ALA198 |
| X | GLU233 |
| X | ASP300 |
| X | HOH608 |
| X | HOH635 |
| X | HOH697 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12527308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299664","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SMD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Deamidated asparagine; partial","evidences":[{"source":"PubMed","id":"1710976","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Deamidated asparagine; partial; alternate","evidences":[{"source":"PubMed","id":"1710976","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1710976","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| X | ASP300 | |
| X | ASP197 | |
| X | GLU233 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| X | ASP197 | |
| X | GLU233 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| X | ASP236 | |
| X | ASP197 |
