1TR1
CRYSTAL STRUCTURE OF E96K MUTATED BETA-GLUCOSIDASE A FROM BACILLUS POLYMYXA, AN ENZYME WITH INCREASED THERMORESISTANCE
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 |
| C | 0000272 | biological_process | polysaccharide catabolic process |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005829 | cellular_component | cytosol |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008422 | molecular_function | beta-glucosidase activity |
| C | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0030245 | biological_process | cellulose catabolic process |
| D | 0000272 | biological_process | polysaccharide catabolic process |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005829 | cellular_component | cytosol |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0008422 | molecular_function | beta-glucosidase activity |
| D | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0030245 | biological_process | cellulose catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 2000 |
| Chain | Residue |
| A | GLN20 |
| A | TYR296 |
| A | TRP326 |
| A | GLU352 |
| A | TRP398 |
| A | GLU405 |
| A | TRP406 |
| A | PHE414 |
| A | HOH2297 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 2000 |
| Chain | Residue |
| B | GLN20 |
| B | TYR296 |
| B | TRP326 |
| B | GLU352 |
| B | TRP398 |
| B | GLU405 |
| B | TRP406 |
| B | PHE414 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 2000 |
| Chain | Residue |
| C | GLN20 |
| C | TYR296 |
| C | TRP326 |
| C | GLU352 |
| C | TRP398 |
| C | GLU405 |
| C | TRP406 |
| C | PHE414 |
| C | HOH2304 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 2000 |
| Chain | Residue |
| D | GLN20 |
| D | TYR296 |
| D | TRP326 |
| D | GLU352 |
| D | TRP398 |
| D | GLU405 |
| D | TRP406 |
| D | PHE414 |
| D | HOH2344 |
Functional Information from PROSITE/UniProt
| site_id | PS00572 |
| Number of Residues | 9 |
| Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGAC |
| Chain | Residue | Details |
| A | ILE348-CYS356 |
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FmWGtAtAAYQiEgA |
| Chain | Residue | Details |
| A | PHE10-ALA24 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10055","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU352 | |
| A | GLU166 | |
| A | ASN294 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU352 | |
| B | GLU166 | |
| B | ARG77 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| C | GLU352 | |
| C | GLU166 | |
| C | ARG77 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| D | GLU352 | |
| D | GLU166 | |
| D | ARG77 |
| site_id | CSA13 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU166 |
| site_id | CSA14 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU166 |
| site_id | CSA15 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| C | GLU166 |
| site_id | CSA16 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| D | GLU166 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU166 | |
| A | ASP265 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU166 | |
| B | ASP265 |
| site_id | CSA19 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| C | GLU166 | |
| C | ASP265 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU352 | |
| B | GLU166 | |
| B | ASN294 |
| site_id | CSA20 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| D | GLU166 | |
| D | ASP265 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| C | GLU352 | |
| C | GLU166 | |
| C | ASN294 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| D | GLU352 | |
| D | GLU166 | |
| D | ASN294 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU166 | |
| A | GLU352 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU166 | |
| B | GLU352 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| C | GLU166 | |
| C | GLU352 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| D | GLU166 | |
| D | GLU352 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU352 | |
| A | GLU166 | |
| A | ARG77 |
