3PBG
6-PHOSPHO-BETA-GALACTOSIDASE FORM-C
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 | 0005990 | biological_process | lactose catabolic 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 | 0019512 | biological_process | lactose catabolic process via tagatose-6-phosphate |
| A | 0033920 | molecular_function | 6-phospho-beta-galactosidase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005990 | biological_process | lactose catabolic 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 | 0019512 | biological_process | lactose catabolic process via tagatose-6-phosphate |
| B | 0033920 | molecular_function | 6-phospho-beta-galactosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 469 |
| Chain | Residue |
| A | TRP347 |
| A | SER428 |
| A | ASN431 |
| A | LYS435 |
| A | TYR437 |
| A | HOH474 |
| A | HOH555 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 469 |
| Chain | Residue |
| B | TRP347 |
| B | SER428 |
| B | ASN431 |
| B | LYS435 |
| B | TYR437 |
| B | HOH484 |
| site_id | ACA |
| Number of Residues | 2 |
| Details | CATALYTIC RESIDUES. |
| Chain | Residue |
| A | GLU160 |
| A | GLU375 |
| site_id | ACB |
| Number of Residues | 2 |
| Details | CATALYTIC RESIDUES. |
| Chain | Residue |
| B | GLU375 |
| B | GLU160 |
| site_id | PHA |
| Number of Residues | 3 |
| Details | PHOSPHATE BINDING SITE. |
| Chain | Residue |
| A | SER428 |
| A | LYS435 |
| A | TYR437 |
| site_id | PHB |
| Number of Residues | 3 |
| Details | PHOSPHATE BINDING SITE. |
| Chain | Residue |
| B | SER428 |
| B | LYS435 |
| B | TYR437 |
Functional Information from PROSITE/UniProt
| site_id | PS00572 |
| Number of Residues | 9 |
| Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGLG |
| Chain | Residue | Details |
| A | ILE371-GLY379 |
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FiFGgAtAAYQaEgA |
| Chain | Residue | Details |
| A | PHE9-ALA23 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01574","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8535789","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01574","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8535789","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01574","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9223646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4PBG","evidenceCode":"ECO:0007744"}]} |
| 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 | GLU375 | |
| A | ASN297 | |
| A | GLU160 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU375 | |
| B | ASN297 | |
| B | GLU160 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU375 | |
| A | GLU160 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU375 | |
| B | GLU160 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 877 |
| Chain | Residue | Details |
| A | GLU160 | proton shuttle (general acid/base) |
| A | GLU375 | covalent catalysis |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 877 |
| Chain | Residue | Details |
| B | GLU160 | proton shuttle (general acid/base) |
| B | GLU375 | covalent catalysis |
