5XXL
Crystal structure of GH3 beta-glucosidase from Bacteroides thetaiotaomicron
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 | 6 |
Details | binding site for residue MG A 801 |
Chain | Residue |
A | ASP699 |
A | VAL701 |
A | HOH935 |
A | HOH938 |
A | HOH995 |
A | HOH1111 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue PEG A 802 |
Chain | Residue |
B | TYR593 |
A | ARG371 |
A | HOH953 |
B | ARG383 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue PG4 A 803 |
Chain | Residue |
A | PHE32 |
A | LEU36 |
A | LYS39 |
A | LEU101 |
A | THR546 |
A | LYS548 |
A | HOH903 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG B 801 |
Chain | Residue |
B | ASP699 |
B | VAL701 |
B | HOH988 |
B | HOH999 |
B | HOH1050 |
B | HOH1076 |
Functional Information from PROSITE/UniProt
site_id | PS00775 |
Number of Residues | 18 |
Details | GLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLRgQwgfnGFVVTDytG |
Chain | Residue | Details |
A | VAL272-GLY289 |