1F4A
E. COLI (LACZ) BETA-GALACTOSIDASE (NCS CONSTRAINED MONOMER-ORTHORHOMBIC)
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 | 7 |
Details | BINDING SITE FOR RESIDUE MG A 3001 |
Chain | Residue |
A | ASN102 |
A | ASP201 |
A | GLU416 |
A | HIS418 |
A | GLU461 |
A | HOH4014 |
A | HOH4156 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 3002 |
Chain | Residue |
A | VAL21 |
A | GLN163 |
A | ASP193 |
A | ASP15 |
A | ASN18 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 3001 |
Chain | Residue |
B | ASN102 |
B | ASP201 |
B | GLU416 |
B | HIS418 |
B | GLU461 |
B | HOH4078 |
B | HOH4198 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 3002 |
Chain | Residue |
B | ASP15 |
B | ASN18 |
B | VAL21 |
B | GLN163 |
B | ASP193 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG C 3001 |
Chain | Residue |
C | ASN102 |
C | ASP201 |
C | GLU416 |
C | HIS418 |
C | GLU461 |
C | HOH4118 |
C | HOH4238 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 3002 |
Chain | Residue |
C | ASP15 |
C | ASN18 |
C | VAL21 |
C | GLN163 |
C | ASP193 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG D 3001 |
Chain | Residue |
D | ASN102 |
D | ASP201 |
D | GLU416 |
D | HIS418 |
D | GLU461 |
D | HOH4014 |
D | HOH4156 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 3002 |
Chain | Residue |
D | ASP15 |
D | ASN18 |
D | VAL21 |
D | GLN163 |
D | ASP193 |
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 |