1JXK
Role of ethe mobile loop in the mehanism of human salivary amylase
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 | 0009311 | biological_process | oligosaccharide metabolic 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 |
| 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 492 |
| Chain | Residue |
| A | ASN100 |
| A | ARG158 |
| A | ASP167 |
| A | HIS201 |
| A | HOH520 |
| A | HOH606 |
| A | HOH618 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 493 |
| Chain | Residue |
| A | ARG332 |
| A | ARG195 |
| A | ASN298 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | ASP197 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | GLU233 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD |
| Chain | Residue | Details |
| A | ASN100 | |
| A | ARG158 | |
| A | ASP167 | |
| A | ARG195 | |
| A | HIS201 | |
| A | ASN298 | |
| A | TYR337 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P04746 |
| Chain | Residue | Details |
| A | ASP300 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000250|UniProtKB:P00687 |
| Chain | Residue | Details |
| A | PCA1 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:1710976 |
| Chain | Residue | Details |
| A | ASN350 | |
| A | GLY459 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Deamidated asparagine; partial; alternate => ECO:0000269|PubMed:1710976 |
| Chain | Residue | Details |
| A | VAL412 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:1710976 |
| Chain | Residue | Details |
| A | VAL412 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | LYS461 |
