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4IPN

The complex structure of 6-phospho-beta-glucosidase BglA-2 with thiocellobiose-6P from Streptococcus pneumoniae

Functional Information from GO Data
ChainGOidnamespacecontents
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0008706molecular_function6-phospho-beta-glucosidase activity
B0016052biological_processcarbohydrate catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
E0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
E0005829cellular_componentcytosol
E0005975biological_processcarbohydrate metabolic process
E0008422molecular_functionbeta-glucosidase activity
E0008706molecular_function6-phospho-beta-glucosidase activity
E0016052biological_processcarbohydrate catabolic process
E0016787molecular_functionhydrolase activity
E0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LFIVENGLG
ChainResidueDetails
BLEU360-GLY368

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGgAvAANQvEgA
ChainResidueDetails
BPHE8-ALA22

238582

PDB entries from 2025-07-09

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