3MI6

Crystal structure of the alpha-galactosidase from Lactobacillus brevis, Northeast Structural Genomics Consortium Target LbR11.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004557	molecular_function	alpha-galactosidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004557	molecular_function	alpha-galactosidase activity
B	0005975	biological_process	carbohydrate metabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0004557	molecular_function	alpha-galactosidase activity
C	0005975	biological_process	carbohydrate metabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0004557	molecular_function	alpha-galactosidase activity
D	0005975	biological_process	carbohydrate metabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Functional Information from PROSITE/UniProt

site_id	PS00512
Number of Residues	16
Details	ALPHA_GALACTOSIDASE Alpha-galactosidase signature. GIemFvLDDg.Wfgh....RD

Chain	Residue	Details
A	GLY360-ASP375

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