5OKA
Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a 6-phospho-beta-galactosidase from Geobacillus stearothermophilus
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0033920 | molecular_function | 6-phospho-beta-galactosidase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0033920 | molecular_function | 6-phospho-beta-galactosidase activity |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0033920 | molecular_function | 6-phospho-beta-galactosidase activity |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0033920 | molecular_function | 6-phospho-beta-galactosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | TRP260 |
| A | ARG369 |
| A | GLN371 |
| A | GOL502 |
| A | HOH905 |
| A | HOH973 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | HOH882 |
| A | TRP260 |
| A | MET262 |
| A | GOL501 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | TYR263 |
| A | GLN265 |
| A | TRP268 |
| A | HOH869 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ASN245 |
| A | ALA266 |
| A | LEU336 |
| A | HOH604 |
| A | HOH626 |
| A | HOH642 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue IMD A 505 |
| Chain | Residue |
| A | ASP59 |
| A | GLU453 |
| A | HOH609 |
| A | HOH814 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| B | TRP260 |
| B | MET262 |
| B | GOL502 |
| B | HOH901 |
| B | HOH957 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | TRP260 |
| B | ARG369 |
| B | GLN371 |
| B | GOL501 |
| B | HOH918 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | TYR263 |
| B | GLN265 |
| B | TRP268 |
| B | TRP285 |
| B | HOH725 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| A | PHE49 |
| A | ASN435 |
| A | HOH665 |
| B | HIS214 |
| B | PRO217 |
| B | HOH602 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| A | HIS214 |
| A | PRO217 |
| B | PHE49 |
| B | ASN435 |
| B | GLN438 |
| B | HOH640 |
| B | HOH714 |
| B | HOH1065 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL C 501 |
| Chain | Residue |
| C | TYR233 |
| C | HIS344 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 502 |
| Chain | Residue |
| C | TYR263 |
| C | GLN265 |
| C | TRP268 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue IMD C 503 |
| Chain | Residue |
| A | HOH640 |
| C | LYS189 |
| C | ASP190 |
| C | HOH938 |
| C | HOH1010 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 501 |
| Chain | Residue |
| D | TYR263 |
| D | GLN265 |
| D | TRP268 |
| D | TRP285 |
| D | HOH921 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue IMD D 502 |
| Chain | Residue |
| C | PRO343 |
| C | HIS344 |
| C | VAL345 |
| C | ASP346 |
| D | GLN156 |
| D | ARG157 |
| D | HOH756 |
Functional Information from PROSITE/UniProt
| site_id | PS00572 |
| Number of Residues | 9 |
| Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. ILITENGLG |
| Chain | Residue | Details |
| A | ILE374-GLY382 |
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGaAsAAYQvEgA |
| Chain | Residue | Details |
| A | PHE13-ALA27 |
