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5BRO

Crystal structure of modified HexB (modB)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001669cellular_componentacrosomal vesicle
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0005975biological_processcarbohydrate metabolic process
A0006044biological_processN-acetylglucosamine metabolic process
A0006491biological_processN-glycan processing
A0006629biological_processlipid metabolic process
A0006689biological_processganglioside catabolic process
A0007338biological_processsingle fertilization
A0008360biological_processregulation of cell shape
A0008375molecular_functionacetylglucosaminyltransferase activity
A0015929molecular_functionhexosaminidase activity
A0016020cellular_componentmembrane
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030203biological_processglycosaminoglycan metabolic process
A0030207biological_processchondroitin sulfate proteoglycan catabolic process
A0030209biological_processdermatan sulfate proteoglycan catabolic process
A0030214biological_processhyaluronan catabolic process
A0030246molecular_functioncarbohydrate binding
A0031410cellular_componentcytoplasmic vesicle
A0035578cellular_componentazurophil granule lumen
A0042582cellular_componentazurophil granule
A0042802molecular_functionidentical protein binding
A0043202cellular_componentlysosomal lumen
A0043615biological_processastrocyte cell migration
A0044877molecular_functionprotein-containing complex binding
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0060473cellular_componentcortical granule
A0070062cellular_componentextracellular exosome
A1901135biological_processcarbohydrate derivative metabolic process
A1905379cellular_componentbeta-N-acetylhexosaminidase complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11329289","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2026-01-28

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