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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3THC

Crystal structure of human beta-galactosidase in complex with galactose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005773cellular_componentvacuole
A0005794cellular_componentGolgi apparatus
A0005975biological_processcarbohydrate metabolic process
A0006516biological_processglycoprotein catabolic process
A0006689biological_processganglioside catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016936molecular_functiongalactoside binding
A0019388biological_processgalactose catabolic process
A0035578cellular_componentazurophil granule lumen
A0042340biological_processkeratan sulfate proteoglycan catabolic process
A0042803molecular_functionprotein homodimerization activity
A0043202cellular_componentlysosomal lumen
A0048471cellular_componentperinuclear region of cytoplasm
A0051413biological_processresponse to cortisone
A0070062cellular_componentextracellular exosome
A1904016biological_processresponse to Thyroglobulin triiodothyronine
A1904813cellular_componentficolin-1-rich granule lumen
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005773cellular_componentvacuole
B0005794cellular_componentGolgi apparatus
B0005975biological_processcarbohydrate metabolic process
B0006516biological_processglycoprotein catabolic process
B0006689biological_processganglioside catabolic process
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016936molecular_functiongalactoside binding
B0019388biological_processgalactose catabolic process
B0035578cellular_componentazurophil granule lumen
B0042340biological_processkeratan sulfate proteoglycan catabolic process
B0042803molecular_functionprotein homodimerization activity
B0043202cellular_componentlysosomal lumen
B0048471cellular_componentperinuclear region of cytoplasm
B0051413biological_processresponse to cortisone
B0070062cellular_componentextracellular exosome
B1904016biological_processresponse to Thyroglobulin triiodothyronine
B1904813cellular_componentficolin-1-rich granule lumen
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0004565molecular_functionbeta-galactosidase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005737cellular_componentcytoplasm
C0005764cellular_componentlysosome
C0005773cellular_componentvacuole
C0005794cellular_componentGolgi apparatus
C0005975biological_processcarbohydrate metabolic process
C0006516biological_processglycoprotein catabolic process
C0006689biological_processganglioside catabolic process
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0016936molecular_functiongalactoside binding
C0019388biological_processgalactose catabolic process
C0035578cellular_componentazurophil granule lumen
C0042340biological_processkeratan sulfate proteoglycan catabolic process
C0042803molecular_functionprotein homodimerization activity
C0043202cellular_componentlysosomal lumen
C0048471cellular_componentperinuclear region of cytoplasm
C0051413biological_processresponse to cortisone
C0070062cellular_componentextracellular exosome
C1904016biological_processresponse to Thyroglobulin triiodothyronine
C1904813cellular_componentficolin-1-rich granule lumen
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0004565molecular_functionbeta-galactosidase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005764cellular_componentlysosome
D0005773cellular_componentvacuole
D0005794cellular_componentGolgi apparatus
D0005975biological_processcarbohydrate metabolic process
D0006516biological_processglycoprotein catabolic process
D0006689biological_processganglioside catabolic process
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0016936molecular_functiongalactoside binding
D0019388biological_processgalactose catabolic process
D0035578cellular_componentazurophil granule lumen
D0042340biological_processkeratan sulfate proteoglycan catabolic process
D0042803molecular_functionprotein homodimerization activity
D0043202cellular_componentlysosomal lumen
D0048471cellular_componentperinuclear region of cytoplasm
D0051413biological_processresponse to cortisone
D0070062cellular_componentextracellular exosome
D1904016biological_processresponse to Thyroglobulin triiodothyronine
D1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS01182
Number of Residues13
DetailsGLYCOSYL_HYDROL_F35 Glycosyl hydrolases family 35 putative active site. GGPVItvQvENEY
ChainResidueDetails
AGLY177-TYR189
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"22128166","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"22128166","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22128166","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24737316","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3THC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22128166","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24737316","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3THC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3THD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22128166","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24737316","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3THC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3THD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22128166","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24737316","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3THC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3THD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WF4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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