1EA9
Cyclomaltodextrinase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005536 | molecular_function | glucose binding |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0005983 | biological_process | starch catabolic process |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047798 | molecular_function | cyclomaltodextrinase activity |
| C | 0051678 | biological_process | pullulan catabolic process |
| C | 2000897 | biological_process | amylopectin catabolic process |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005536 | molecular_function | glucose binding |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0005983 | biological_process | starch catabolic process |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047798 | molecular_function | cyclomaltodextrinase activity |
| D | 0051678 | biological_process | pullulan catabolic process |
| D | 2000897 | biological_process | amylopectin catabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P38940 |
| Chain | Residue | Details |
| C | ASP325 | |
| D | ASP325 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P38940 |
| Chain | Residue | Details |
| C | GLU354 | |
| D | GLU354 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P38940 |
| Chain | Residue | Details |
| C | ASN143 | |
| D | GLY168 | |
| D | ASP170 | |
| D | HIS243 | |
| D | ARG323 | |
| D | HIS420 | |
| D | ASP465 | |
| D | ARG469 | |
| C | GLY168 | |
| C | ASP170 | |
| C | HIS243 | |
| C | ARG323 | |
| C | HIS420 | |
| C | ASP465 | |
| C | ARG469 | |
| D | ASN143 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P13507 |
| Chain | Residue | Details |
| C | ASP421 | |
| D | ASP421 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP325 | |
| C | GLU354 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| D | ASP325 | |
| D | GLU354 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP465 | |
| C | ASP325 | |
| C | ASP390 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| D | ASP465 | |
| D | ASP325 | |
| D | ASP390 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | TRP356 | |
| C | ASP325 | |
| C | ASP421 | |
| C | GLU354 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| D | TRP356 | |
| D | ASP325 | |
| D | ASP421 | |
| D | GLU354 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP421 | |
| C | ASP325 | |
| C | GLU354 | |
| C | HIS243 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| D | ASP421 | |
| D | ASP325 | |
| D | GLU354 | |
| D | HIS243 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP421 | |
| C | ASP325 | |
| C | GLU354 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| D | ASP421 | |
| D | ASP325 | |
| D | GLU354 |
| site_id | CSA11 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| C | ASP325 | |
| C | ASP421 | |
| C | ARG323 | |
| C | GLU354 | |
| C | HIS420 |
| site_id | CSA12 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| D | ASP325 | |
| D | ASP421 | |
| D | ARG323 | |
| D | GLU354 | |
| D | HIS420 |
