8ZRZ
The 1.26 angstrom resolution structure of Bacillus cereus beta-amylase in complex with maltose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0005976 | biological_process | polysaccharide metabolic process |
| A | 0016161 | molecular_function | beta-amylase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0046872 | molecular_function | metal ion binding |
| A | 2001070 | molecular_function | starch binding |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 102 |
| Details | Domain: {"description":"CBM20","evidences":[{"source":"PROSITE-ProRule","id":"PRU00594","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10353816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12761294","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10353816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12761294","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10353816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12761294","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10353816","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
