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6SD0

Structure of beta-galactosidase from Thermotoga maritima.

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate 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
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate 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
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0030246molecular_functioncarbohydrate 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
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 1101
ChainResidue
AALA511
AGLY513
AGLY575
AGLU584
AGLU586

site_idAC2
Number of Residues5
Detailsbinding site for residue MG B 1101
ChainResidue
BGLU586
BALA511
BGLY513
BGLY575
BGLU584

site_idAC3
Number of Residues5
Detailsbinding site for residue MG C 1101
ChainResidue
CALA511
CGLY513
CGLY575
CGLU584
CGLU586

site_idAC4
Number of Residues5
Detailsbinding site for residue MG D 1101
ChainResidue
DALA511
DGLY513
DGLY575
DGLU584
DGLU586

Functional Information from PROSITE/UniProt
site_idPS00608
Number of Residues15
DetailsGLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPSIIFWSlg.NE
ChainResidueDetails
AASP427-GLU441

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NtVRTSHYPnqtkWYdlcDyfGLYVI
ChainResidueDetails
AASN363-ILE388

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU441
BGLU441
CGLU441
DGLU441

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AGLU507
BGLU507
CGLU507
DGLU507

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PDB entries from 2024-05-15

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