3J7H
Structure of beta-galactosidase at 3.2-A resolution obtained by cryo-electron microscopy
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 | 0009056 | biological_process | 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 | 0009056 | biological_process | 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 | 0009056 | biological_process | 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 | 0009056 | biological_process | 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 PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 3001 |
Chain | Residue |
A | GLU416 |
A | HIS418 |
A | GLU461 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 3001 |
Chain | Residue |
B | GLU416 |
B | HIS418 |
B | GLU461 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 3001 |
Chain | Residue |
C | GLU416 |
C | HIS418 |
C | GLU461 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG D 3001 |
Chain | Residue |
D | GLU416 |
D | HIS418 |
D | GLU461 |
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 | GLU461 | |
B | GLU461 | |
C | GLU461 | |
D | GLU461 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:1350782 |
Chain | Residue | Details |
A | GLU537 | |
B | GLU537 | |
C | GLU537 | |
D | GLU537 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN102 | |
B | GLU461 | |
B | GLU537 | |
B | PHE601 | |
B | ASN604 | |
B | TRP999 | |
C | ASN102 | |
C | ASP201 | |
C | GLU461 | |
C | GLU537 | |
C | PHE601 | |
A | ASP201 | |
C | ASN604 | |
C | TRP999 | |
D | ASN102 | |
D | ASP201 | |
D | GLU461 | |
D | GLU537 | |
D | PHE601 | |
D | ASN604 | |
D | TRP999 | |
A | GLU461 | |
A | GLU537 | |
A | PHE601 | |
A | ASN604 | |
A | TRP999 | |
B | ASN102 | |
B | ASP201 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11045615 |
Chain | Residue | Details |
A | GLU416 | |
D | GLU416 | |
D | HIS418 | |
D | ASN597 | |
A | HIS418 | |
A | ASN597 | |
B | GLU416 | |
B | HIS418 | |
B | ASN597 | |
C | GLU416 | |
C | HIS418 | |
C | ASN597 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | HIS357 | |
A | HIS391 | |
B | HIS357 | |
B | HIS391 | |
C | HIS357 | |
C | HIS391 | |
D | HIS357 | |
D | 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 |
A | TRP999 | |
B | TRP999 | |
C | TRP999 | |
D | TRP999 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
A | ASP201 | |
A | ASN604 | |
A | HIS357 | |
A | HIS391 | |
A | GLU416 | |
A | HIS418 | |
A | GLU461 | |
A | GLU537 | |
A | ASN597 | |
A | PHE601 |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
B | ASP201 | |
B | ASN604 | |
B | HIS357 | |
B | HIS391 | |
B | GLU416 | |
B | HIS418 | |
B | GLU461 | |
B | GLU537 | |
B | ASN597 | |
B | PHE601 |
site_id | MCSA3 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
C | ASP201 | |
C | ASN604 | |
C | HIS357 | |
C | HIS391 | |
C | GLU416 | |
C | HIS418 | |
C | GLU461 | |
C | GLU537 | |
C | ASN597 | |
C | PHE601 |
site_id | MCSA4 |
Number of Residues | 10 |
Details | M-CSA 422 |
Chain | Residue | Details |
D | ASP201 | |
D | ASN604 | |
D | HIS357 | |
D | HIS391 | |
D | GLU416 | |
D | HIS418 | |
D | GLU461 | |
D | GLU537 | |
D | ASN597 | |
D | PHE601 |