1PX4
E. COLI (LACZ) BETA-GALACTOSIDASE (G794A) WITH IPTG BOUND
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0031420 | molecular_function | alkali metal ion binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium 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 | 0031420 | molecular_function | alkali metal ion binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0004565 | molecular_function | beta-galactosidase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0005990 | biological_process | lactose catabolic process |
| C | 0009341 | cellular_component | beta-galactosidase complex |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0031420 | molecular_function | alkali metal ion binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0004565 | molecular_function | beta-galactosidase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0005990 | biological_process | lactose catabolic process |
| D | 0009341 | cellular_component | beta-galactosidase complex |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0031420 | molecular_function | alkali metal ion binding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00608 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DRNHPSVIIWSlg.NE |
| Chain | Residue | Details |
| A | ASP447-GLU461 |
| site_id | PS00719 |
| Number of Residues | 26 |
| Details | GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaVRCSHYPnhplWYtlcDryGLYVV |
| Chain | Residue | Details |
| A | ASN385-VAL410 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:6420154 |
| Chain | Residue | Details |
| A | SER462 | |
| B | SER462 | |
| C | SER462 | |
| D | SER462 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:1350782 |
| Chain | Residue | Details |
| A | TYR538 | |
| B | TYR538 | |
| C | TYR538 | |
| D | TYR538 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | VAL103 | |
| B | SER462 | |
| B | TYR538 | |
| B | CYS602 | |
| B | GLY605 | |
| B | SER1000 | |
| C | VAL103 | |
| C | MET202 | |
| C | SER462 | |
| C | TYR538 | |
| C | CYS602 | |
| A | MET202 | |
| C | GLY605 | |
| C | SER1000 | |
| D | VAL103 | |
| D | MET202 | |
| D | SER462 | |
| D | TYR538 | |
| D | CYS602 | |
| D | GLY605 | |
| D | SER1000 | |
| A | SER462 | |
| A | TYR538 | |
| A | CYS602 | |
| A | GLY605 | |
| A | SER1000 | |
| B | VAL103 | |
| B | MET202 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11045615 |
| Chain | Residue | Details |
| A | THR417 | |
| D | THR417 | |
| D | GLY419 | |
| D | ASP598 | |
| A | GLY419 | |
| A | ASP598 | |
| B | THR417 | |
| B | GLY419 | |
| B | ASP598 | |
| C | THR417 | |
| C | GLY419 | |
| C | ASP598 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | GLU358 | |
| A | TYR392 | |
| B | GLU358 | |
| B | TYR392 | |
| C | GLU358 | |
| C | TYR392 | |
| D | GLU358 | |
| D | TYR392 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | SITE: Important for ensuring that an appropriate proportion of lactose is converted to allolactose |
| Chain | Residue | Details |
| A | SER1000 | |
| B | SER1000 | |
| C | SER1000 | |
| D | SER1000 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bgl |
| Chain | Residue | Details |
| A | GLU461 | |
| A | GLU537 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bgl |
| Chain | Residue | Details |
| B | GLU461 | |
| B | GLU537 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bgl |
| Chain | Residue | Details |
| C | GLU461 | |
| C | GLU537 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bgl |
| Chain | Residue | Details |
| D | GLU461 | |
| D | GLU537 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bgl |
| Chain | Residue | Details |
| A | TYR503 | |
| A | GLU461 | |
| A | GLU537 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bgl |
| Chain | Residue | Details |
| B | TYR503 | |
| B | GLU461 | |
| B | GLU537 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bgl |
| Chain | Residue | Details |
| C | TYR503 | |
| C | GLU461 | |
| C | GLU537 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bgl |
| Chain | Residue | Details |
| D | TYR503 | |
| D | GLU461 | |
| D | GLU537 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 422 |
| Chain | Residue | Details |
| A | MET202 | |
| A | GLY605 | |
| A | GLU358 | |
| A | TYR392 | |
| A | THR417 | |
| A | GLY419 | |
| A | SER462 | |
| A | TYR538 | |
| A | ASP598 | |
| A | CYS602 |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 422 |
| Chain | Residue | Details |
| B | MET202 | |
| B | GLY605 | |
| B | GLU358 | |
| B | TYR392 | |
| B | THR417 | |
| B | GLY419 | |
| B | SER462 | |
| B | TYR538 | |
| B | ASP598 | |
| B | CYS602 |
| site_id | MCSA3 |
| Number of Residues | 10 |
| Details | M-CSA 422 |
| Chain | Residue | Details |
| C | MET202 | |
| C | GLY605 | |
| C | GLU358 | |
| C | TYR392 | |
| C | THR417 | |
| C | GLY419 | |
| C | SER462 | |
| C | TYR538 | |
| C | ASP598 | |
| C | CYS602 |
| site_id | MCSA4 |
| Number of Residues | 10 |
| Details | M-CSA 422 |
| Chain | Residue | Details |
| D | MET202 | |
| D | GLY605 | |
| D | GLU358 | |
| D | TYR392 | |
| D | THR417 | |
| D | GLY419 | |
| D | SER462 | |
| D | TYR538 | |
| D | ASP598 | |
| D | CYS602 |
