1BG9
BARLEY ALPHA-AMYLASE WITH SUBSTRATE ANALOGUE ACARBOSE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004556 | molecular_function | alpha-amylase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005983 | biological_process | starch catabolic process |
| A | 0005987 | biological_process | sucrose catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0043169 | molecular_function | cation binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AS |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| A | ASP179 |
| A | GLU204 |
| A | ASP289 |
| site_id | SS |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| A | TRP276 |
| A | TRP277 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8196040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9634702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AVA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00693","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | GLU204 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | ASP233 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | GLU204 | |
| A | TRP206 | |
| A | ASP289 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | GLU204 | |
| A | ASP179 | |
| A | ARG177 | |
| A | ASP289 | |
| A | HIS288 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | GLU204 | |
| A | ASP179 | |
| A | HIS92 | |
| A | ASP289 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | GLU204 | |
| A | ASP289 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP179 | |
| A | ASP289 | |
| A | GLU227 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 397 |
| Chain | Residue | Details |
| A | ASP179 | covalent catalysis |
| A | GLU204 | hydrogen radical acceptor, proton shuttle (general acid/base) |
| A | ASP289 | electrostatic stabiliser, hydrogen radical acceptor, proton shuttle (general acid/base) |
