1DED
CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION
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 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 | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP27 | |
| A | ASN193 | |
| A | ASP199 | |
| A | ASN233 | |
| A | ASP371 | |
| A | ARG375 | |
| B | ASP27 | |
| B | ASN29 | |
| B | ASN32 | |
| B | ASN33 | |
| B | GLY51 | |
| A | ASN29 | |
| B | ASP53 | |
| B | TYR100 | |
| B | ASN139 | |
| B | ILE190 | |
| B | ASN193 | |
| B | ASP199 | |
| B | ASN233 | |
| B | ASP371 | |
| B | ARG375 | |
| A | ASN32 | |
| A | ASN33 | |
| A | GLY51 | |
| A | ASP53 | |
| A | TYR100 | |
| A | ASN139 | |
| A | ILE190 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS140 | |
| A | ARG227 | |
| A | LYS232 | |
| A | HIS327 | |
| B | HIS140 | |
| B | ARG227 | |
| B | LYS232 | |
| B | HIS327 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP328 | |
| B | ASP328 |
