6R5I
The crystal structure of the Glycoside Hydrolase BglX from P. aeruginosa
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 | 8 |
Details | binding site for residue SO4 A 801 |
Chain | Residue |
A | ASP110 |
A | PHE154 |
A | MET251 |
A | ASP286 |
A | MET318 |
A | HOH971 |
A | HOH1079 |
A | HOH1100 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 802 |
Chain | Residue |
A | VAL694 |
A | HOH944 |
A | HOH982 |
A | HOH1026 |
A | HOH1031 |
A | ASP692 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 801 |
Chain | Residue |
B | ARG629 |
B | ALA634 |
B | ASN635 |
B | HOH1241 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue SO4 B 802 |
Chain | Residue |
B | ASP110 |
B | PHE154 |
B | LYS207 |
B | ASP286 |
B | TRP429 |
B | HOH971 |
B | HOH1083 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG B 803 |
Chain | Residue |
B | ASP692 |
B | VAL694 |
B | HOH990 |
B | HOH1021 |
B | HOH1073 |
B | HOH1119 |
Functional Information from PROSITE/UniProt
site_id | PS00775 |
Number of Residues | 18 |
Details | GLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. LLRqQwgfkGLTISDhgA |
Chain | Residue | Details |
A | LEU272-ALA289 |