1PPI
THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION
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 | 0008152 | biological_process | 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 |
Functional Information from PDB Data
| site_id | AS1 |
| Number of Residues | 3 |
| Details | ACTIVE SITE 1 |
| Chain | Residue |
| A | VAL163 |
| A | GLN63 |
| A | LEU165 |
| site_id | AS2 |
| Number of Residues | 3 |
| Details | ACTIVE SITE 2 |
| Chain | Residue |
| A | HIS305 |
| A | GLN63 |
| A | TRP59 |
| site_id | AS3 |
| Number of Residues | 4 |
| Details | ACTIVE SITE 3 |
| Chain | Residue |
| A | HIS101 |
| A | ASP300 |
| A | HIS299 |
| A | ASP197 |
| site_id | AS4 |
| Number of Residues | 3 |
| Details | ACTIVE SITE 4 |
| Chain | Residue |
| A | HIS201 |
| A | GLU233 |
| A | ASP300 |
| site_id | AS5 |
| Number of Residues | 2 |
| Details | ACTIVE SITE 5 |
| Chain | Residue |
| A | GLU240 |
| A | LYS200 |
| site_id | CAL |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE |
| Chain | Residue |
| A | ASN100 |
| A | ARG158 |
| A | ASP167 |
| A | HIS201 |
| site_id | CLO |
| Number of Residues | 3 |
| Details | CHLORIDE BINDING SITE |
| Chain | Residue |
| A | ARG195 |
| A | ASN298 |
| A | ARG337 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | ASP212 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | PHE248 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631 |
| Chain | Residue | Details |
| A | CYS115 | |
| A | ASP173 | |
| A | TYR182 | |
| A | ASN216 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631 |
| Chain | Residue | Details |
| A | VAL210 | |
| A | GLU352 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | LEU313 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P04746 |
| Chain | Residue | Details |
| A | PHE315 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000250|UniProtKB:P04746 |
| Chain | Residue | Details |
| A | LEU16 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
| Chain | Residue | Details |
| A | ILE427 |
