Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic 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 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 |