1PX8

Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase

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	0008152	biological_process	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	0008152	biological_process	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 PROSITE/UniProt

site_id	PS01027
Number of Residues	10
Details	GLYCOSYL_HYDROL_F39 Glycosyl hydrolases family 39 active site. WpFEiWNEPN

Chain	Residue	Details
A	TRP153-ASN162

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10068

Chain	Residue	Details
A	GLU160
B	GLU160

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:9761746

Chain	Residue	Details
A	GLU277
B	GLU277

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