5VA9
Human pancreatic alpha amylase in complex with peptide inhibitor piHA-L5(d10Y)
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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004556 | molecular_function | alpha-amylase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0031404 | molecular_function | chloride ion binding |
| B | 0043169 | molecular_function | cation binding |
| B | 0044245 | biological_process | polysaccharide digestion |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | ARG195 |
| A | ASN298 |
| A | ARG337 |
| A | HOH671 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | HOH657 |
| A | ASN100 |
| A | ARG158 |
| A | ASP167 |
| A | HIS201 |
| A | HOH636 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 501 |
| Chain | Residue |
| B | ARG195 |
| B | ASN298 |
| B | ARG337 |
| B | HOH687 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 502 |
| Chain | Residue |
| B | ASN100 |
| B | ARG158 |
| B | ASP167 |
| B | HIS201 |
| B | HOH624 |
| B | HOH655 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for Di-peptide ACE C 0 and TYR C 1 |
| Chain | Residue |
| A | SER145 |
| C | GLY2 |
| C | HIS13 |
| C | TYR16 |
| C | CYS17 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide ACE C 0 and CYS C 17 |
| Chain | Residue |
| C | TYR1 |
| C | GLY2 |
| C | HIS13 |
| C | VAL14 |
| C | SER15 |
| C | TYR16 |
| C | GLY18 |
| C | NH219 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for Di-peptide GLY C 18 and NH2 C 19 |
| Chain | Residue |
| C | VAL14 |
| C | SER15 |
| C | TYR16 |
| C | CYS17 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide ACE D 0 and CYS D 17 |
| Chain | Residue |
| A | GLN349 |
| D | TYR1 |
| D | GLY2 |
| D | HIS13 |
| D | VAL14 |
| D | TYR16 |
| D | GLY18 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide ACE D 0 and TYR D 1 |
| Chain | Residue |
| A | TYR276 |
| B | SER145 |
| B | GLU149 |
| D | GLY2 |
| D | HIS13 |
| D | TYR16 |
| D | CYS17 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for Di-peptide GLY D 18 and NH2 D 19 |
| Chain | Residue |
| D | VAL14 |
| D | TYR16 |
| D | CYS17 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| 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 | 2 |
| 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 | 14 |
| 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 | 2 |
| 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 | 2 |
| 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 |
