5ZQX

Crystal structure of beta-xylosidase mutant (E186Q) 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
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
C	0009044	molecular_function	xylan 1,4-beta-xylosidase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0045493	biological_process	xylan catabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005975	biological_process	carbohydrate metabolic process
D	0009044	molecular_function	xylan 1,4-beta-xylosidase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0045493	biological_process	xylan catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250\|UniProtKB:A7LXU0

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250\|UniProtKB:A7LXU0

site_id	SWS_FT_FI3
Number of Residues	4
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