4IIH

Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with thiocellobiose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0008422	molecular_function	beta-glucosidase activity
A	0009251	biological_process	glucan catabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0030245	biological_process	cellulose catabolic process
B	0000272	biological_process	polysaccharide catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0008422	molecular_function	beta-glucosidase activity
B	0009251	biological_process	glucan catabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0030245	biological_process	cellulose catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00775
Number of Residues	18
Details	GLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. LLKaElgfqGFVMSDwgA

Chain	Residue	Details
A	LEU266-ALA283

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	30
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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