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6TTE

Beta-galactosidase in complex with PETG

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0005990biological_processlactose catabolic process
A0009341cellular_componentbeta-galactosidase complex
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0031420molecular_functionalkali metal ion binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0005975biological_processcarbohydrate metabolic process
B0005990biological_processlactose catabolic process
B0009341cellular_componentbeta-galactosidase complex
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
B0031420molecular_functionalkali metal ion binding
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0004565molecular_functionbeta-galactosidase activity
C0005975biological_processcarbohydrate metabolic process
C0005990biological_processlactose catabolic process
C0009341cellular_componentbeta-galactosidase complex
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0030246molecular_functioncarbohydrate binding
C0031420molecular_functionalkali metal ion binding
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0004565molecular_functionbeta-galactosidase activity
D0005975biological_processcarbohydrate metabolic process
D0005990biological_processlactose catabolic process
D0009341cellular_componentbeta-galactosidase complex
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0030246molecular_functioncarbohydrate binding
D0031420molecular_functionalkali metal ion binding
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 3001
ChainResidue
AGLU416
AHIS418
AGLU461
AHOH3113
AHOH3144
AHOH3162

site_idAC2
Number of Residues12
Detailsbinding site for residue PTQ A 3002
ChainResidue
ATYR503
AGLU537
AHIS540
AASP598
AASN604
ATRP999
AHOH3113
AHOH3302
AHOH3319
AASN102
AASP201
AGLU461

site_idAC3
Number of Residues6
Detailsbinding site for residue MG B 3001
ChainResidue
BGLU416
BHIS418
BGLU461
BHOH3113
BHOH3144
BHOH3162

site_idAC4
Number of Residues12
Detailsbinding site for residue PTQ B 3002
ChainResidue
BASN102
BASP201
BGLU461
BTYR503
BGLU537
BHIS540
BASP598
BASN604
BTRP999
BHOH3113
BHOH3302
BHOH3319

site_idAC5
Number of Residues6
Detailsbinding site for residue MG C 3001
ChainResidue
CGLU416
CHIS418
CGLU461
CHOH3113
CHOH3144
CHOH3162

site_idAC6
Number of Residues12
Detailsbinding site for residue PTQ C 3002
ChainResidue
CASN102
CASP201
CGLU461
CTYR503
CGLU537
CHIS540
CASP598
CASN604
CTRP999
CHOH3113
CHOH3302
CHOH3319

site_idAC7
Number of Residues6
Detailsbinding site for residue MG D 3001
ChainResidue
DGLU416
DHIS418
DGLU461
DHOH3113
DHOH3144
DHOH3162

site_idAC8
Number of Residues12
Detailsbinding site for residue PTQ D 3002
ChainResidue
DASN102
DASP201
DGLU461
DTYR503
DGLU537
DHIS540
DASP598
DASN604
DTRP999
DHOH3113
DHOH3302
DHOH3319

Functional Information from PROSITE/UniProt
site_idPS00608
Number of Residues15
DetailsGLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DRNHPSVIIWSlg.NE
ChainResidueDetails
AASP447-GLU461

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaVRCSHYPnhplWYtlcDryGLYVV
ChainResidueDetails
AASN385-VAL410

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01687","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01687","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01687","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01687","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Important for ensuring that an appropriate proportion of lactose is converted to allolactose"}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 422
ChainResidueDetails
AASP201
AASN604
AHIS357
AHIS391
AGLU416
AHIS418
AGLU461
AGLU537
AASN597
APHE601

site_idMCSA2
Number of Residues10
DetailsM-CSA 422
ChainResidueDetails
BASP201
BASN604
BHIS357
BHIS391
BGLU416
BHIS418
BGLU461
BGLU537
BASN597
BPHE601

site_idMCSA3
Number of Residues10
DetailsM-CSA 422
ChainResidueDetails
CASP201
CASN604
CHIS357
CHIS391
CGLU416
CHIS418
CGLU461
CGLU537
CASN597
CPHE601

site_idMCSA4
Number of Residues10
DetailsM-CSA 422
ChainResidueDetails
DASP201
DASN604
DHIS357
DHIS391
DGLU416
DHIS418
DGLU461
DGLU537
DASN597
DPHE601

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PDB entries from 2025-07-23

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