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4IPL

The crystal structure of 6-phospho-beta-glucosidase BglA-2 from Streptococcus pneumoniae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0008706molecular_function6-phospho-beta-glucosidase activity
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
ATRP338
AMET423
ASER424
ALYS430
ATYR432
AHOH846

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LFIVENGLG
ChainResidueDetails
ALEU360-GLY368

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGgAvAANQvEgA
ChainResidueDetails
APHE8-ALA22

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PDB entries from 2025-12-24

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