Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004556 | molecular_function | alpha-amylase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0043169 | molecular_function | cation binding |
A | 0043895 | molecular_function | cyclomaltodextrin glucanotransferase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 2001070 | molecular_function | starch binding |
Functional Information from PDB Data
site_id | CA1 |
Number of Residues | 6 |
Details | 1ST CALCIUM BINDING SITE |
Chain | Residue |
A | ASP27 |
A | ASN29 |
A | ASN32 |
A | ASN33 |
A | GLY51 |
A | ASP53 |
site_id | CA2 |
Number of Residues | 4 |
Details | 2ND CALCIUM BINDING SITE |
Chain | Residue |
A | ASN139 |
A | ILE190 |
A | ASP199 |
A | HIS233 |
site_id | CAT |
Number of Residues | 3 |
Details | CATALYTIC SITE |
Chain | Residue |
A | ASP229 |
A | GLU257 |
A | ASP328 |
site_id | MB1 |
Number of Residues | 5 |
Details | FIRST MALTOSE-BINDING SITE |
Chain | Residue |
A | TRP616 |
A | LYS651 |
A | TRP662 |
A | GLU663 |
A | ASN667 |
site_id | MB2 |
Number of Residues | 7 |
Details | 2ND MALTOSE-BINDING SITE |
Chain | Residue |
A | THR598 |
A | ALA599 |
A | GLY601 |
A | ASN603 |
A | ASN627 |
A | GLN628 |
A | TYR633 |
site_id | MB3 |
Number of Residues | 10 |
Details | 3RD MALTOSE-BINDING SITE |
Chain | Residue |
A | TYR301 |
A | GLU411 |
A | ARG412 |
A | TRP413 |
A | ILE414 |
A | GLY446 |
A | VAL448 |
A | SER537 |
A | ALA539 |
A | ASP540 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | ASP229 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | GLU257 | |
site_id | SWS_FT_FI3 |
Number of Residues | 21 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP27 | |
A | SER145 | |
A | ILE190 | |
A | ASN193 | |
A | ASP199 | |
A | ARG227 | |
A | LYS232 | |
A | HIS233 | |
A | ALA315 | |
A | HIS327 | |
A | ASP371 | |
A | ASN29 | |
A | ARG375 | |
A | ASP577 | |
A | ASN32 | |
A | ASN33 | |
A | GLY51 | |
A | ASP53 | |
A | TYR100 | |
A | ASN139 | |
A | HIS140 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000250 |
Chain | Residue | Details |
A | ASP328 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | THR254 | |
A | ASP229 | |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | ASP328 | |
A | GLU257 | |
A | ASP229 | |
A | ARG227 | |
A | HIS327 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | ASP229 | |
A | GLU257 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | ASP328 | |
A | GLU257 | |
A | ASP229 | |
A | HIS140 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | ASP328 | |
A | ASP229 | |
A | GLU257 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | GLU264 | |
A | ASP229 | |
A | ASP319 | |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1amy |
Chain | Residue | Details |
A | PHE259 | |
A | ASP328 | |
A | ASP229 | |
A | GLU257 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 45 |
Chain | Residue | Details |
A | ARG227 | electrostatic stabiliser, hydrogen bond donor |
A | ASP229 | nucleofuge, nucleophile |
A | GLU257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | HIS327 | electrostatic stabiliser, hydrogen bond donor |
A | ASP328 | electrostatic stabiliser, hydrogen bond acceptor |