2J7B
Beta-glucosidase from Thermotoga maritima in complex with gluco- tetrazole
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008422 | molecular_function | beta-glucosidase activity |
A | 0016052 | biological_process | carbohydrate catabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0030245 | biological_process | cellulose catabolic process |
A | 0102483 | molecular_function | scopolin beta-glucosidase activity |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008422 | molecular_function | beta-glucosidase activity |
B | 0016052 | biological_process | carbohydrate catabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0030245 | biological_process | cellulose catabolic process |
B | 0102483 | molecular_function | scopolin beta-glucosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A1447 |
Chain | Residue |
A | VAL53 |
A | ALA54 |
A | TYR410 |
A | TYR421 |
A | GLN424 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT B1447 |
Chain | Residue |
B | TYR177 |
B | PHE267 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CA B1448 |
Chain | Residue |
B | ASP278 |
B | SER281 |
B | GLU282 |
B | HOH2221 |
B | HOH2222 |
B | HOH2226 |
A | HOH2158 |
A | HOH2159 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NTZ A1446 |
Chain | Residue |
A | GLN20 |
A | HIS121 |
A | ASN165 |
A | GLU166 |
A | TYR295 |
A | TRP324 |
A | GLU351 |
A | TRP398 |
A | GLU405 |
A | TRP406 |
A | PHE414 |
A | HOH2431 |
A | HOH2432 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NTZ B1446 |
Chain | Residue |
B | GLN20 |
B | HIS121 |
B | ASN165 |
B | GLU166 |
B | TYR295 |
B | TRP324 |
B | GLU351 |
B | TRP398 |
B | GLU405 |
B | TRP406 |
B | PHE414 |
B | HOH2134 |
B | HOH2304 |
B | HOH2305 |
Functional Information from PROSITE/UniProt
site_id | PS00572 |
Number of Residues | 9 |
Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. VYITENGAA |
Chain | Residue | Details |
A | VAL347-ALA355 |
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGvAtASYQiEgS |
Chain | Residue | Details |
A | PHE10-SER24 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255 |
Chain | Residue | Details |
A | GLU166 | |
B | GLU166 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 |
Chain | Residue | Details |
A | GLU351 | |
B | GLU351 |