5OSS
Beta-glucosidase from Thermotoga maritima in complex with Gluco-1H-imidazole
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 | 3 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | ALA54 |
| A | TYR421 |
| A | HOH650 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | ALA144 |
| A | GLU145 |
| A | ARG148 |
| A | HOH664 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | TRP142 |
| A | THR90 |
| A | LYS131 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | GLY43 |
| A | LYS46 |
| A | ALA407 |
| A | HOH702 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | ARG240 |
| A | LYS337 |
| A | HOH603 |
| A | HOH609 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | TYR177 |
| A | PHE267 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | GLN20 |
| A | GLU166 |
| A | TYR295 |
| A | TRP324 |
| A | GLU351 |
| A | TRP398 |
| A | GLU405 |
| A | TRP406 |
| A | PHE414 |
| A | HOH653 |
| A | HOH703 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 508 |
| Chain | Residue |
| A | ARG137 |
| A | HOH718 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | VAL53 |
| B | ALA54 |
| B | TYR410 |
| B | TYR421 |
| B | HOH601 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| A | GLU110 |
| B | ARG137 |
| B | ARG199 |
| B | ARG203 |
| B | ASP279 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | TYR177 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 504 |
| Chain | Residue |
| B | ASP278 |
| B | GLU282 |
| B | HOH627 |
| B | HOH712 |
| B | HOH735 |
| site_id | AD4 |
| Number of Residues | 12 |
| Details | binding site for residue AEZ B 505 |
| 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 | HOH614 |
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 |
