5IDI
Structure of beta glucosidase 1A from Thermotoga neapolitana, mutant E349A
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 |
| A | 0031217 | molecular_function | glucan 1,4-beta-glucosidase activity |
| 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 |
| B | 0031217 | molecular_function | glucan 1,4-beta-glucosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ACT A 501 |
| Chain | Residue |
| A | GLN18 |
| A | TRP396 |
| A | GLU403 |
| A | TRP404 |
| A | HOH667 |
| A | HOH669 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 502 |
| Chain | Residue |
| A | HOH638 |
| A | HOH769 |
| A | SER294 |
| A | HIS296 |
| A | TRP322 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 501 |
| Chain | Residue |
| B | GLN18 |
| B | TRP396 |
| B | GLU403 |
| B | TRP404 |
| B | HOH665 |
| B | HOH666 |
Functional Information from PROSITE/UniProt
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGvAtASYQiEgS |
| Chain | Residue | Details |
| A | PHE8-SER22 |
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 |
