5ZQS

Crystal structure of beta-xylosidase mutant (E186Q/F503Y) from Bacillus pumilus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0009044	molecular_function	xylan 1,4-beta-xylosidase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0045493	biological_process	xylan catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0009044	molecular_function	xylan 1,4-beta-xylosidase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0045493	biological_process	xylan catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:A7LXU0

Chain	Residue	Details
A	ASP14
B	ASP14

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:A7LXU0

Chain	Residue	Details
A	GLN186
B	GLN186

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000250|UniProtKB:A7LXU0

Chain	Residue	Details
A	ASP127
B	ASP127

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