5DT7
Crystal structure of the GH1 beta-glucosidase from Exiguobacterium antarcticum B7 in space group C2221
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008422 | molecular_function | beta-glucosidase activity |
| A | 0030245 | biological_process | cellulose catabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008422 | molecular_function | beta-glucosidase activity |
| B | 0030245 | biological_process | cellulose catabolic process |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008422 | molecular_function | beta-glucosidase activity |
| C | 0030245 | biological_process | cellulose catabolic process |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0008422 | molecular_function | beta-glucosidase activity |
| D | 0030245 | biological_process | cellulose catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue CXS A 501 |
| Chain | Residue |
| A | SER305 |
| A | ASP306 |
| A | HOH608 |
| A | HOH613 |
| B | HIS172 |
| B | ASP306 |
| B | PHE307 |
| B | CXS501 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | HIS180 |
| A | GOL504 |
| A | HIS125 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | GLY277 |
| A | ASP278 |
| A | LEU279 |
| A | ALA280 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ILE31 |
| A | THR34 |
| A | PHE35 |
| A | THR38 |
| A | HIS125 |
| A | PRO178 |
| A | SO4502 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ILE251 |
| A | PHE252 |
| A | SER283 |
| A | THR284 |
| A | PRO285 |
| A | CYS286 |
| A | LEU344 |
| A | HOH636 |
| A | HOH708 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CXS B 501 |
| Chain | Residue |
| A | ASP306 |
| A | PHE307 |
| A | HIS309 |
| A | CXS501 |
| B | SER305 |
| B | ASP306 |
| B | HOH619 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | HIS125 |
| B | HIS180 |
| B | GOL503 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | ILE31 |
| B | THR34 |
| B | THR38 |
| B | PRO178 |
| B | SO4502 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue CXS C 501 |
| Chain | Residue |
| C | HIS172 |
| C | ALA304 |
| C | SER305 |
| C | SER305 |
| C | ASP306 |
| C | ASP306 |
| C | HIS309 |
| C | HOH610 |
| C | HOH626 |
| C | HOH683 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 502 |
| Chain | Residue |
| C | HIS125 |
| C | HIS180 |
| C | GOL504 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 503 |
| Chain | Residue |
| C | ALA276 |
| C | GLY277 |
| C | ASP278 |
| C | LEU279 |
| C | ALA280 |
| C | HOH652 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 504 |
| Chain | Residue |
| C | ILE31 |
| C | THR34 |
| C | THR38 |
| C | HIS125 |
| C | PRO178 |
| C | SO4502 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue CXS D 501 |
| Chain | Residue |
| D | LEU173 |
| D | SER305 |
| D | SER305 |
| D | ASP306 |
| D | ASP306 |
| D | HIS309 |
| D | HOH603 |
| D | HOH622 |
| D | HOH677 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 502 |
| Chain | Residue |
| D | HIS125 |
| D | HIS180 |
| D | GOL504 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 503 |
| Chain | Residue |
| D | ALA276 |
| D | GLY277 |
| D | LEU279 |
| D | ALA280 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 504 |
| Chain | Residue |
| D | ILE31 |
| D | THR34 |
| D | PHE35 |
| D | THR38 |
| D | PRO178 |
| D | SO4502 |
Functional Information from PROSITE/UniProt
| site_id | PS00572 |
| Number of Residues | 9 |
| Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGAA |
| Chain | Residue | Details |
| A | ILE346-ALA354 |
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FvFGtAtSSYQiEgA |
| Chain | Residue | Details |
| A | PHE7-ALA21 |
