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5WAB

Crystal Structure of Bifidobacterium adolescentis GH3 beta-glucosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009251biological_processglucan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0009251biological_processglucan catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0008422molecular_functionbeta-glucosidase activity
C0009251biological_processglucan catabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0008422molecular_functionbeta-glucosidase activity
D0009251biological_processglucan catabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 801
ChainResidue
AASP44
ALEU106
AARG120
ALYS153
AHIS154
AMET197
AASP232

Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLRdEwgyeGIVMSDwgA
ChainResidueDetails
AVAL218-ALA235

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PDB entries from 2024-06-12

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