Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3E1F

E.Coli (lacZ) beta-galactosidase (H418E) in complex with galactose

Functional Information from GO Data
ChainGOidnamespacecontents
10000287molecular_functionmagnesium ion binding
10003824molecular_functioncatalytic activity
10004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
10004565molecular_functionbeta-galactosidase activity
10005975biological_processcarbohydrate metabolic process
10005990biological_processlactose catabolic process
10009341cellular_componentbeta-galactosidase complex
10016798molecular_functionhydrolase activity, acting on glycosyl bonds
10030246molecular_functioncarbohydrate binding
10031420molecular_functionalkali metal ion binding
10042802molecular_functionidentical protein binding
10046872molecular_functionmetal ion binding
20000287molecular_functionmagnesium ion binding
20003824molecular_functioncatalytic activity
20004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
20004565molecular_functionbeta-galactosidase activity
20005975biological_processcarbohydrate metabolic process
20005990biological_processlactose catabolic process
20009341cellular_componentbeta-galactosidase complex
20016798molecular_functionhydrolase activity, acting on glycosyl bonds
20030246molecular_functioncarbohydrate binding
20031420molecular_functionalkali metal ion binding
20042802molecular_functionidentical protein binding
20046872molecular_functionmetal ion binding
30000287molecular_functionmagnesium ion binding
30003824molecular_functioncatalytic activity
30004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
30004565molecular_functionbeta-galactosidase activity
30005975biological_processcarbohydrate metabolic process
30005990biological_processlactose catabolic process
30009341cellular_componentbeta-galactosidase complex
30016798molecular_functionhydrolase activity, acting on glycosyl bonds
30030246molecular_functioncarbohydrate binding
30031420molecular_functionalkali metal ion binding
30042802molecular_functionidentical protein binding
30046872molecular_functionmetal ion binding
40000287molecular_functionmagnesium ion binding
40003824molecular_functioncatalytic activity
40004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
40004565molecular_functionbeta-galactosidase activity
40005975biological_processcarbohydrate metabolic process
40005990biological_processlactose catabolic process
40009341cellular_componentbeta-galactosidase complex
40016798molecular_functionhydrolase activity, acting on glycosyl bonds
40030246molecular_functioncarbohydrate binding
40031420molecular_functionalkali metal ion binding
40042802molecular_functionidentical protein binding
40046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00608
Number of Residues15
DetailsGLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DRNHPSVIIWSlg.NE
ChainResidueDetails
1ASP447-GLU461

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaVRCSHYPnhplWYtlcDryGLYVV
ChainResidueDetails
1ASN385-VAL410

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:6420154
ChainResidueDetails
1GLU461
2GLU461
3GLU461
4GLU461

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:1350782
ChainResidueDetails
1GLU537
2GLU537
3GLU537
4GLU537

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING:
ChainResidueDetails
2ASN102
2ASP201
2GLU461
2GLU537
2PHE601
2ASN604
2TRP999
3ASN102
3ASP201
3GLU461
3GLU537
3PHE601
3ASN604
3TRP999
4ASN102
4ASP201
4GLU461
4GLU537
4PHE601
4ASN604
4TRP999
1ASN102
1ASP201
1GLU461
1GLU537
1PHE601
1ASN604
1TRP999

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:11045615
ChainResidueDetails
1GLU416
1GLU418
2GLU416
2GLU418
3GLU416
3GLU418
4GLU416
4GLU418
1ASN597
2ASN597
3ASN597
4ASN597

site_idSWS_FT_FI5
Number of Residues8
DetailsSITE: Transition state stabilizer
ChainResidueDetails
3HIS357
3HIS391
4HIS357
4HIS391
1HIS357
1HIS391
2HIS357
2HIS391

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Important for ensuring that an appropriate proportion of lactose is converted to allolactose
ChainResidueDetails
1TRP999
2TRP999
3TRP999
4TRP999

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 422
ChainResidueDetails
1HIS357
1HIS391
1GLU416
1GLU418
1GLU461
1GLU537
1ASN597
1PHE601
1ASN604
1ASP201

site_idMCSA2
Number of Residues10
DetailsM-CSA 422
ChainResidueDetails
2ASP201
2HIS357
2HIS391
2GLU416
2GLU418
2GLU461
2GLU537
2ASN597
2PHE601
2ASN604

site_idMCSA3
Number of Residues10
DetailsM-CSA 422
ChainResidueDetails
3ASP201
3HIS357
3HIS391
3GLU416
3GLU418
3GLU461
3GLU537
3ASN597
3PHE601
3ASN604

site_idMCSA4
Number of Residues10
DetailsM-CSA 422
ChainResidueDetails
4ASP201
4HIS357
4HIS391
4GLU416
4GLU418
4GLU461
4GLU537
4ASN597
4PHE601
4ASN604

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon