4X0N
Porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004556 | molecular_function | alpha-amylase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016160 | molecular_function | amylase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0031404 | molecular_function | chloride ion binding |
| A | 0043169 | molecular_function | cation binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0015066 | molecular_function | alpha-amylase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | ARG195 |
| A | ASN298 |
| A | ARG337 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | HOH807 |
| A | ASN100 |
| A | ARG158 |
| A | ASP167 |
| A | HIS201 |
| A | HOH805 |
| A | HOH806 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | TRP58 |
| A | ASP300 |
| A | ARG303 |
| A | HIS305 |
| A | GLY306 |
| A | ASP356 |
| B | TYR1007 |
| B | GLY1011 |
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 | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8193143","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8681972","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8994970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| 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_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Region: {"description":"Inhibitory motif","evidences":[{"source":"PubMed","id":"27066537","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
