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 | 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 |
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 | 0016160 | molecular_function | amylase 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 | ACT_SITE: Nucleophile => ECO:0000305|PubMed:10091666, ECO:0000305|PubMed:10769135, ECO:0000305|PubMed:11914097 |
Chain | Residue | Details |
A | ASP197 | |
B | ASP197 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
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 | GLU233 | |
B | GLU233 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
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 | |
B | ASP167 | |
B | ARG195 | |
B | HIS201 | |
B | ASN298 | |
B | ARG337 | |
A | ARG158 | |
A | ASP167 | |
A | ARG195 | |
A | HIS201 | |
A | ASN298 | |
A | ARG337 | |
B | ASN100 | |
B | ARG158 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:10091666, ECO:0000305|PubMed:10769135, ECO:0000305|PubMed:11914097 |
Chain | Residue | Details |
A | ASP300 | |
B | ASP300 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:11772019, ECO:0000269|PubMed:8528071 |
Chain | Residue | Details |
A | PCA1 | |
B | PCA1 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10091666, ECO:0000269|PubMed:10769135, ECO:0000269|PubMed:11772019 |
Chain | Residue | Details |
A | ASN461 | |
B | ASN461 |