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 | 0016740 | molecular_function | transferase activity |
| 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004556 | molecular_function | alpha-amylase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0043169 | molecular_function | cation binding |
| B | 0043895 | molecular_function | cyclomaltodextrin glucanotransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 2001070 | molecular_function | starch binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 687 |
| Chain | Residue |
| A | ASP27 |
| A | ASN29 |
| A | ASN32 |
| A | ASN33 |
| A | GLY51 |
| A | ASP53 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 688 |
| Chain | Residue |
| A | ASN139 |
| A | ILE190 |
| A | ASP199 |
| A | HIS233 |
| A | HOH698 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 687 |
| Chain | Residue |
| B | ASP27 |
| B | ASN29 |
| B | ASN32 |
| B | ASN33 |
| B | GLY51 |
| B | ASP53 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 688 |
| Chain | Residue |
| B | ILE190 |
| B | ASP199 |
| B | HIS233 |
| 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 | CA3 |
| Number of Residues | 6 |
| Details | 1ST CALCIUM BINDING SITE. |
| Chain | Residue |
| B | ASP27 |
| B | ASN29 |
| B | ASN32 |
| B | ASN33 |
| B | GLY51 |
| B | ASP53 |
| site_id | CA4 |
| Number of Residues | 4 |
| Details | 2ND CALCIUM BINDING SITE. |
| Chain | Residue |
| B | ASN139 |
| B | ILE190 |
| B | ASP199 |
| B | HIS233 |
| site_id | CT1 |
| Number of Residues | 3 |
| Details | CATALYTIC SITE. |
| Chain | Residue |
| A | ASP229 |
| A | GLU257 |
| A | ASP328 |
| site_id | CT2 |
| Number of Residues | 3 |
| Details | CATALYTIC SITE. |
| Chain | Residue |
| B | ASP229 |
| B | GLU257 |
| B | ASP328 |
| site_id | MB1 |
| Number of Residues | 5 |
| Details | 1ST MALTOSE BINDING SITE. SITE MB1 ALSO INCLUDES RESIDUE SER 382 FROM A SYMMETRY-RELATED MOLECULE. |
| Chain | Residue |
| A | ALA616 |
| 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 | 7 |
| Details | 3RD MALTOSE BINDING SITE. SITE MB3 ALSO INCLUDES RESIDUES SER 537, ALA 539, ASP 540 FROM A SYMMETRY-RELATED MOLECULE. |
| Chain | Residue |
| A | TYR301 |
| A | GLU411 |
| A | ARG412 |
| A | TRP413 |
| A | ILE414 |
| A | GLY446 |
| A | VAL448 |
| site_id | MB4 |
| Number of Residues | 6 |
| Details | 1ST MALTOSE BINDING SITE. |
| Chain | Residue |
| B | SER382 |
| B | ALA616 |
| B | LYS651 |
| B | TRP662 |
| B | GLU663 |
| B | ASN667 |
| site_id | MB5 |
| Number of Residues | 7 |
| Details | 2ND MALTOSE BINDING SITE. |
| Chain | Residue |
| B | THR598 |
| B | ALA599 |
| B | GLY601 |
| B | ASN603 |
| B | ASN627 |
| B | GLN628 |
| B | TYR633 |
| site_id | MB6 |
| Number of Residues | 10 |
| Details | 3RD MALTOSE BINDING SITE, # - DENOTES SYMMETRY-RELATED MOLECULE. |
| Chain | Residue |
| B | TYR301 |
| B | GLU411 |
| B | ARG412 |
| B | TRP413 |
| B | ILE414 |
| B | GLY446 |
| B | VAL448 |
| B | SER537 |
| B | ALA539 |
| B | ASP540 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | ASP229 | |
| B | ASP229 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | GLU257 | |
| B | GLU257 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 42 |
| 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 | |
| B | ASP27 | |
| B | ASN29 | |
| B | ASN32 | |
| B | ASN33 | |
| B | GLY51 | |
| B | ASP53 | |
| B | TYR100 | |
| B | ASN139 | |
| A | ASN32 | |
| B | HIS140 | |
| B | SER145 | |
| B | ILE190 | |
| B | ASN193 | |
| B | ASP199 | |
| B | ARG227 | |
| B | LYS232 | |
| B | HIS233 | |
| B | ALA315 | |
| B | HIS327 | |
| A | ASN33 | |
| B | ASP371 | |
| B | ARG375 | |
| B | ASP577 | |
| A | GLY51 | |
| A | ASP53 | |
| A | TYR100 | |
| A | ASN139 | |
| A | HIS140 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP328 | |
| B | 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 | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP328 | |
| B | ASP229 | |
| B | GLU257 | |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | GLU264 | |
| A | ASP229 | |
| A | ASP319 | |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | GLU264 | |
| B | ASP229 | |
| B | ASP319 | |
| site_id | CSA13 |
| 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 | CSA14 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | PHE259 | |
| B | ASP328 | |
| B | ASP229 | |
| B | GLU257 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | THR254 | |
| B | ASP229 | |
| site_id | CSA3 |
| 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 | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP328 | |
| B | GLU257 | |
| B | ASP229 | |
| B | ARG227 | |
| B | HIS327 | |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP229 | |
| A | GLU257 | |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP229 | |
| B | GLU257 | |
| site_id | CSA7 |
| 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 | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP328 | |
| B | GLU257 | |
| B | ASP229 | |
| B | HIS140 | |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| 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 |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 45 |
| Chain | Residue | Details |
| B | ARG227 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP229 | nucleofuge, nucleophile |
| B | GLU257 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS327 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP328 | electrostatic stabiliser, hydrogen bond acceptor |
