1VEP
Crystal Structure Analysis of Triple (T47M/Y164E/T328N)/maltose of Bacillus cereus Beta-Amylase at pH 6.5
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0046872 | molecular_function | metal ion binding |
A | 0102229 | molecular_function | amylopectin maltohydrolase activity |
A | 2001070 | molecular_function | starch binding |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10050, ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294 |
Chain | Residue | Details |
A | GLU172 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294 |
Chain | Residue | Details |
A | GLU367 |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294 |
Chain | Residue | Details |
A | THR330 | |
A | ARG397 | |
A | ASP49 | |
A | HIS89 | |
A | ASP97 | |
A | LYS287 | |
A | HIS292 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10353816 |
Chain | Residue | Details |
A | GLU56 | |
A | ASP60 | |
A | GLN61 | |
A | GLU141 | |
A | GLU144 | |
A | ASN368 |