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 | 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 | 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 | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000305|PubMed:8535789 |
Chain | Residue | Details |
A | GLU160 | |
B | GLU160 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000305|PubMed:8535789 |
Chain | Residue | Details |
A | GLU375 | |
B | GLU375 |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG |
Chain | Residue | Details |
A | GLN19 | |
B | GLN19 | |
B | HIS116 | |
B | ASN159 | |
B | GLU160 | |
B | ASN297 | |
B | SER428 | |
B | TRP429 | |
B | LYS435 | |
B | TYR437 | |
A | HIS116 | |
A | ASN159 | |
A | GLU160 | |
A | ASN297 | |
A | SER428 | |
A | TRP429 | |
A | LYS435 | |
A | TYR437 |
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 |