2WBK

Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004567	molecular_function	beta-mannosidase activity
A	0005576	cellular_component	extracellular region
A	0005764	cellular_component	lysosome
A	0005975	biological_process	carbohydrate metabolic process
A	0006516	biological_process	glycoprotein 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	0004567	molecular_function	beta-mannosidase activity
B	0005576	cellular_component	extracellular region
B	0005764	cellular_component	lysosome
B	0005975	biological_process	carbohydrate metabolic process
B	0006516	biological_process	glycoprotein catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1bgl

Chain	Residue	Details
A	GLU462
A	GLN555

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1bgl

Chain	Residue	Details
B	GLU462
B	GLN555

---