1BVN
PIG PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE PROTEINACEOUS INHIBITOR TENDAMISTAT
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| P | 0003824 | molecular_function | catalytic activity |
| P | 0004556 | molecular_function | alpha-amylase activity |
| P | 0005509 | molecular_function | calcium ion binding |
| P | 0005576 | cellular_component | extracellular region |
| P | 0005615 | cellular_component | extracellular space |
| P | 0005975 | biological_process | carbohydrate metabolic process |
| P | 0008152 | biological_process | metabolic process |
| P | 0016052 | biological_process | carbohydrate catabolic process |
| P | 0016160 | molecular_function | amylase activity |
| P | 0016787 | molecular_function | hydrolase activity |
| P | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| P | 0031404 | molecular_function | chloride ion binding |
| P | 0043169 | molecular_function | cation binding |
| P | 0046872 | molecular_function | metal ion binding |
| T | 0015066 | molecular_function | alpha-amylase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA P 2001 |
| Chain | Residue |
| P | ASN100 |
| P | ARG158 |
| P | ASP167 |
| P | HIS201 |
| P | HOH1152 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL P 2002 |
| Chain | Residue |
| P | ARG195 |
| P | ARG337 |
| site_id | AS |
| Number of Residues | 3 |
| Details | CATALYTICALLY ACTIVE RESIDUES. |
| Chain | Residue |
| P | ASP197 |
| P | GLU233 |
| P | ASP300 |
| site_id | CA |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE. |
| Chain | Residue |
| P | ASN100 |
| P | ARG158 |
| P | ASP167 |
| P | HIS201 |
| site_id | CL |
| Number of Residues | 3 |
| Details | CHLORIDE BINDING SITE. |
| Chain | Residue |
| P | ARG337 |
| P | ARG195 |
| P | ASN298 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| P | ASP212 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| P | 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 |
| P | CYS115 | |
| P | ASP173 | |
| P | TYR182 | |
| P | 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 |
| P | VAL210 | |
| P | GLU352 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| P | LEU313 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P04746 |
| Chain | Residue | Details |
| P | PHE315 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000250|UniProtKB:P04746 |
| Chain | Residue | Details |
| P | LEU16 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
| Chain | Residue | Details |
| P | ILE427 |
