4ZOA
Crystal Structure of beta-glucosidase from Listeria innocua in complex with isofagomine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008422 | molecular_function | beta-glucosidase activity |
A | 0009251 | biological_process | glucan catabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0046872 | molecular_function | metal ion binding |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008422 | molecular_function | beta-glucosidase activity |
B | 0009251 | biological_process | glucan catabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue IFM A 801 |
Chain | Residue |
A | THR40 |
A | ASP91 |
A | PHE135 |
A | ARG149 |
A | LYS191 |
A | HIS192 |
A | ASP270 |
A | GLU473 |
A | HOH1000 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 802 |
Chain | Residue |
A | ASP648 |
A | THR650 |
A | HOH930 |
A | HOH997 |
A | HOH1003 |
A | HOH1144 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue PEG B 801 |
Chain | Residue |
A | TRP470 |
A | ARG481 |
A | HOH1070 |
B | LEU588 |
B | HOH1178 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue IFM B 802 |
Chain | Residue |
B | THR40 |
B | ASP91 |
B | PHE135 |
B | ARG149 |
B | LYS191 |
B | HIS192 |
B | ASP270 |
B | GLU473 |
B | HOH1081 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG B 803 |
Chain | Residue |
B | ASP648 |
B | THR650 |
B | HOH933 |
B | HOH961 |
B | HOH985 |
B | HOH1128 |
Functional Information from PROSITE/UniProt
site_id | PS00775 |
Number of Residues | 18 |
Details | GLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLRgEmefdGVLISDwgA |
Chain | Residue | Details |
A | VAL256-ALA273 |