7M1R
Crystal structure of a 6-phospho-beta-galactosidase from Bacillus licheniformis
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 501 |
Chain | Residue |
A | TYR123 |
A | ASN174 |
A | PRO185 |
A | HOH708 |
A | HOH721 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | HOH705 |
A | GLU170 |
A | TYR173 |
A | TYR301 |
A | HOH682 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | ARG93 |
A | TYR135 |
A | ARG142 |
A | GLU145 |
A | ASP146 |
A | HOH789 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO B 501 |
Chain | Residue |
B | TYR123 |
B | ASN174 |
B | PRO185 |
B | HOH701 |
B | HOH799 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | GLU170 |
B | TYR173 |
B | TYR301 |
B | HOH729 |
B | HOH761 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | ARG93 |
B | TYR135 |
B | ARG142 |
B | GLU145 |
B | ASP146 |
B | HOH636 |
B | HOH834 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue EDO C 501 |
Chain | Residue |
C | TYR123 |
C | ASN174 |
C | PHE175 |
C | PRO185 |
C | HOH684 |
C | HOH741 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO C 502 |
Chain | Residue |
C | GLU170 |
C | TYR173 |
C | TYR301 |
C | HOH690 |
C | HOH783 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue EDO C 503 |
Chain | Residue |
C | ARG93 |
C | ARG142 |
C | GLU145 |
C | ASP146 |
C | HOH760 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO D 501 |
Chain | Residue |
D | GLU170 |
D | TYR173 |
D | TYR301 |
D | TRP352 |
D | HOH638 |
Functional Information from PROSITE/UniProt
site_id | PS00572 |
Number of Residues | 9 |
Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LFITENGLG |
Chain | Residue | Details |
A | LEU374-GLY382 |
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGsAsAAYQiEgA |
Chain | Residue | Details |
A | PHE13-ALA27 |