1KGW
THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE
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 | 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 | 0044245 | biological_process | polysaccharide digestion |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10091666","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10769135","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11914097","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10091666","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10769135","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11772019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11914097","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10091666","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10769135","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11772019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8528071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HNY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"10091666","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10769135","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11914097","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10091666","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10769135","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11772019","evidenceCode":"ECO:0000269"}]} |
| 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 |
| A | ASP300 | |
| A | ASP197 | |
| A | GLU233 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP197 | |
| A | GLU233 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP236 | |
| A | ASP197 |
