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2JFE

The crystal structure of human cytosolic beta-glucosidase

Functional Information from GO Data
ChainGOidnamespacecontents
X0004336molecular_functiongalactosylceramidase activity
X0004348molecular_functionglucosylceramidase activity
X0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
X0004565molecular_functionbeta-galactosidase activity
X0005515molecular_functionprotein binding
X0005737cellular_componentcytoplasm
X0005829cellular_componentcytosol
X0005975biological_processcarbohydrate metabolic process
X0006629biological_processlipid metabolic process
X0006680biological_processglucosylceramide catabolic process
X0006683biological_processgalactosylceramide catabolic process
X0008422molecular_functionbeta-glucosidase activity
X0009313biological_processoligosaccharide catabolic process
X0016020cellular_componentmembrane
X0016139biological_processglycoside catabolic process
X0016798molecular_functionhydrolase activity, acting on glycosyl bonds
X0017042molecular_functionglycosylceramidase activity
X0046477biological_processglycosylceramide catabolic process
X0046479biological_processglycosphingolipid catabolic process
X0050821biological_processprotein stabilization
X1901805biological_processbeta-glucoside catabolic process
X1902494cellular_componentcatalytic complex
X1903017biological_processpositive regulation of exo-alpha-sialidase activity
Functional Information from PROSITE/UniProt
site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FgWAaAtAAYQvEgG
ChainResidueDetails
XPHE7-GLY21

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
XGLU165

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255
ChainResidueDetails
XGLU373

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
XGLN17
XHIS120
XASN164
XTYR309
XTRP417

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
XGLU424

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
XGLU373
XGLU165
XGLN307

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
XGLU165
XGLU373

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PDB entries from 2024-11-06

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