1KBB
Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
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 | 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 PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 497 |
| Chain | Residue |
| A | ASN100 |
| A | ARG158 |
| A | ASP167 |
| A | HIS201 |
| A | HOH806 |
| A | HOH839 |
| A | HOH843 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 498 |
| Chain | Residue |
| A | ARG337 |
| A | ARG195 |
| A | ASN298 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:10091666, ECO:0000305|PubMed:10769135, ECO:0000305|PubMed:11914097 |
| Chain | Residue | Details |
| A | ASP197 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:10091666, ECO:0000305|PubMed:10769135, ECO:0000305|PubMed:11772019, ECO:0000305|PubMed:11914097 |
| Chain | Residue | Details |
| A | ALA233 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:8528071, ECO:0007744|PDB:1HNY |
| Chain | Residue | Details |
| A | ASN100 | |
| A | ARG158 | |
| A | ASP167 | |
| A | ARG195 | |
| A | HIS201 | |
| A | ASN298 | |
| A | ARG337 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:10091666, ECO:0000305|PubMed:10769135, ECO:0000305|PubMed:11914097 |
| Chain | Residue | Details |
| A | ASP300 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:8528071 |
| Chain | Residue | Details |
| A | PCA1 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019 |
| Chain | Residue | Details |
| A | ASN461 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1m53 |
| Chain | Residue | Details |
| A | ASP236 | |
| A | ASP197 |
