3E1F
E.Coli (lacZ) beta-galactosidase (H418E) in complex with galactose
Functional Information from GO Data
Chain | GOid | namespace | contents |
1 | 0000287 | molecular_function | magnesium ion binding |
1 | 0003824 | molecular_function | catalytic activity |
1 | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
1 | 0004565 | molecular_function | beta-galactosidase activity |
1 | 0005975 | biological_process | carbohydrate metabolic process |
1 | 0005990 | biological_process | lactose catabolic process |
1 | 0009056 | biological_process | catabolic process |
1 | 0009341 | cellular_component | beta-galactosidase complex |
1 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
1 | 0030246 | molecular_function | carbohydrate binding |
1 | 0031420 | molecular_function | alkali metal ion binding |
1 | 0042802 | molecular_function | identical protein binding |
1 | 0046872 | molecular_function | metal ion binding |
2 | 0000287 | molecular_function | magnesium ion binding |
2 | 0003824 | molecular_function | catalytic activity |
2 | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
2 | 0004565 | molecular_function | beta-galactosidase activity |
2 | 0005975 | biological_process | carbohydrate metabolic process |
2 | 0005990 | biological_process | lactose catabolic process |
2 | 0009056 | biological_process | catabolic process |
2 | 0009341 | cellular_component | beta-galactosidase complex |
2 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
2 | 0030246 | molecular_function | carbohydrate binding |
2 | 0031420 | molecular_function | alkali metal ion binding |
2 | 0042802 | molecular_function | identical protein binding |
2 | 0046872 | molecular_function | metal ion binding |
3 | 0000287 | molecular_function | magnesium ion binding |
3 | 0003824 | molecular_function | catalytic activity |
3 | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
3 | 0004565 | molecular_function | beta-galactosidase activity |
3 | 0005975 | biological_process | carbohydrate metabolic process |
3 | 0005990 | biological_process | lactose catabolic process |
3 | 0009056 | biological_process | catabolic process |
3 | 0009341 | cellular_component | beta-galactosidase complex |
3 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
3 | 0030246 | molecular_function | carbohydrate binding |
3 | 0031420 | molecular_function | alkali metal ion binding |
3 | 0042802 | molecular_function | identical protein binding |
3 | 0046872 | molecular_function | metal ion binding |
4 | 0000287 | molecular_function | magnesium ion binding |
4 | 0003824 | molecular_function | catalytic activity |
4 | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
4 | 0004565 | molecular_function | beta-galactosidase activity |
4 | 0005975 | biological_process | carbohydrate metabolic process |
4 | 0005990 | biological_process | lactose catabolic process |
4 | 0009056 | biological_process | catabolic process |
4 | 0009341 | cellular_component | beta-galactosidase complex |
4 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
4 | 0030246 | molecular_function | carbohydrate binding |
4 | 0031420 | molecular_function | alkali metal ion binding |
4 | 0042802 | molecular_function | identical protein binding |
4 | 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 |
1 | ASP447-GLU461 |
site_id | PS00719 |
Number of Residues | 26 |
Details | GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaVRCSHYPnhplWYtlcDryGLYVV |
Chain | Residue | Details |
1 | 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 |
1 | GLU461 | |
2 | GLU461 | |
3 | GLU461 | |
4 | GLU461 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:1350782 |
Chain | Residue | Details |
1 | GLU537 | |
2 | GLU537 | |
3 | GLU537 | |
4 | GLU537 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
1 | ASN102 | |
2 | GLU461 | |
2 | GLU537 | |
2 | PHE601 | |
2 | ASN604 | |
2 | TRP999 | |
3 | ASN102 | |
3 | ASP201 | |
3 | GLU461 | |
3 | GLU537 | |
3 | PHE601 | |
1 | ASP201 | |
3 | ASN604 | |
3 | TRP999 | |
4 | ASN102 | |
4 | ASP201 | |
4 | GLU461 | |
4 | GLU537 | |
4 | PHE601 | |
4 | ASN604 | |
4 | TRP999 | |
1 | GLU461 | |
1 | GLU537 | |
1 | PHE601 | |
1 | ASN604 | |
1 | TRP999 | |
2 | ASN102 | |
2 | ASP201 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11045615 |
Chain | Residue | Details |
1 | GLU416 | |
4 | GLU416 | |
4 | GLU418 | |
4 | ASN597 | |
1 | GLU418 | |
1 | ASN597 | |
2 | GLU416 | |
2 | GLU418 | |
2 | ASN597 | |
3 | GLU416 | |
3 | GLU418 | |
3 | ASN597 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
1 | HIS357 | |
1 | HIS391 | |
2 | HIS357 | |
2 | HIS391 | |
3 | HIS357 | |
3 | HIS391 | |
4 | HIS357 | |
4 | HIS391 |
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 |
1 | TRP999 | |
2 | TRP999 | |
3 | TRP999 | |
4 | TRP999 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
1 | GLU461 | |
1 | GLU537 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
2 | GLU461 | |
2 | GLU537 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
3 | GLU461 | |
3 | GLU537 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
4 | GLU461 | |
4 | GLU537 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
1 | TYR503 | |
1 | GLU461 | |
1 | GLU537 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
2 | TYR503 | |
2 | GLU461 | |
2 | GLU537 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
3 | TYR503 | |
3 | GLU461 | |
3 | GLU537 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bgl |
Chain | Residue | Details |
4 | TYR503 | |
4 | GLU461 | |
4 | GLU537 |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
1 | ASP201 | |
1 | ASN604 | |
1 | HIS357 | |
1 | HIS391 | |
1 | GLU416 | |
1 | GLU418 | |
1 | GLU461 | |
1 | GLU537 | |
1 | ASN597 | |
1 | PHE601 |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
2 | ASP201 | |
2 | ASN604 | |
2 | HIS357 | |
2 | HIS391 | |
2 | GLU416 | |
2 | GLU418 | |
2 | GLU461 | |
2 | GLU537 | |
2 | ASN597 | |
2 | PHE601 |
site_id | MCSA3 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
3 | ASP201 | |
3 | ASN604 | |
3 | HIS357 | |
3 | HIS391 | |
3 | GLU416 | |
3 | GLU418 | |
3 | GLU461 | |
3 | GLU537 | |
3 | ASN597 | |
3 | PHE601 |
site_id | MCSA4 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
4 | ASP201 | |
4 | ASN604 | |
4 | HIS357 | |
4 | HIS391 | |
4 | GLU416 | |
4 | GLU418 | |
4 | GLU461 | |
4 | GLU537 | |
4 | ASN597 | |
4 | PHE601 |