3BGA
Crystal structure of beta-galactosidase from Bacteroides thetaiotaomicron VPI-5482
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0004565 | molecular_function | beta-galactosidase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0005990 | biological_process | lactose catabolic process |
A | 0009341 | cellular_component | beta-galactosidase complex |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0004565 | molecular_function | beta-galactosidase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0005990 | biological_process | lactose catabolic process |
B | 0009341 | cellular_component | beta-galactosidase complex |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0030246 | molecular_function | carbohydrate binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1 |
Chain | Residue |
A | GLU438 |
A | HIS440 |
A | GLU484 |
A | HOH1476 |
A | HOH1477 |
A | HOH1478 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 2 |
Chain | Residue |
B | HOH1462 |
B | HOH1463 |
B | HOH1465 |
B | GLU438 |
B | HIS440 |
B | GLU484 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 3 |
Chain | Residue |
B | ASP227 |
B | PHE614 |
B | ASN617 |
B | HOH1039 |
B | HOH1603 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 4 |
Chain | Residue |
A | ASP227 |
A | PHE614 |
A | ASN617 |
A | HOH1054 |
A | HOH1589 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 5 |
Chain | Residue |
B | PRO924 |
B | LEU966 |
B | GLU967 |
B | ALA969 |
B | HOH1470 |
B | HOH1547 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 6 |
Chain | Residue |
A | PRO924 |
A | LEU966 |
A | GLU967 |
A | ALA969 |
A | HOH1099 |
A | HOH1520 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 7 |
Chain | Residue |
A | LYS192 |
A | THR193 |
A | ASN436 |
A | HOH1179 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 8 |
Chain | Residue |
B | LYS192 |
B | THR193 |
B | ASN436 |
Functional Information from PROSITE/UniProt
site_id | PS00719 |
Number of Residues | 26 |
Details | GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NmVRNSHYPthpyWYqlcDryGLYMI |
Chain | Residue | Details |
A | ASN407-ILE432 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
A | GLU548 | |
A | GLU484 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
B | GLU548 | |
B | GLU484 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
A | TYR521 | |
A | GLU548 | |
A | GLU484 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
B | TYR521 | |
B | GLU548 | |
B | GLU484 |