5OGZ
Crystal structure of Ruminiclostridium Thermocellum beta-Glucosidase A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| 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 | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030245 | biological_process | cellulose catabolic process |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| 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 | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030245 | biological_process | cellulose catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | LYS302 |
| A | PRO313 |
| A | ALA314 |
| A | ASN315 |
| A | SER316 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| B | ARG137 |
| B | LYS203 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | ALA314 |
| B | ASN315 |
| B | SER316 |
| B | LYS302 |
| B | PRO313 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | SER224 |
| B | TYR225 |
| B | ASN295 |
| B | SER297 |
| B | SER298 |
| B | GLY334 |
| B | LEU335 |
| B | TYR382 |
| B | HOH624 |
Functional Information from PROSITE/UniProt
| site_id | PS00572 |
| Number of Residues | 9 |
| Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IVISENGAA |
| Chain | Residue | Details |
| A | ILE351-ALA359 |
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FiWGsAtAAYQiEgA |
| Chain | Residue | Details |
| A | PHE10-ALA24 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10055","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
