Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0016161 | molecular_function | beta-amylase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 1490 |
Chain | Residue |
A | THR127 |
A | ASN129 |
A | PRO188 |
A | PRO191 |
A | TYR236 |
A | HOH2492 |
A | HOH2943 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 1491 |
Chain | Residue |
A | GLU228 |
A | PHE229 |
A | HOH2945 |
A | HOH2947 |
A | HOH2948 |
A | GLN212 |
A | PHE215 |
Functional Information from PROSITE/UniProt
site_id | PS00506 |
Number of Residues | 9 |
Details | BETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD |
Chain | Residue | Details |
A | HIS91-ASP99 | |
site_id | PS00679 |
Number of Residues | 11 |
Details | BETA_AMYLASE_2 Beta-amylase active site 2. GpAGEMRYPSY |
Chain | Residue | Details |
A | GLY180-TYR190 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU184 | |
Chain | Residue | Details |
A | GLU378 | |
Chain | Residue | Details |
A | ASP51 | |
A | HIS91 | |
A | ASP99 | |
A | LYS293 | |
A | HIS298 | |
A | THR340 | |
A | ASN379 | |
A | ARG418 | |