5ZQS

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

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	0009044	molecular_function	xylan 1,4-beta-xylosidase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0045493	biological_process	xylan 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	0009044	molecular_function	xylan 1,4-beta-xylosidase activity
B	0016787	molecular_function	hydrolase 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	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"A7LXU0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"A7LXU0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate","evidences":[{"source":"UniProtKB","id":"A7LXU0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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