2F6B

Structural and active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp. (NCL 87-6-10).

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	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031176	molecular_function	endo-1,4-beta-xylanase activity
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	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0031176	molecular_function	endo-1,4-beta-xylanase activity
B	0045493	biological_process	xylan catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00776
Number of Residues	11
Details	GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEYYIVDsW

Chain	Residue	Details
A	PRO91-TRP101

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site_id	PS00777
Number of Residues	12
Details	GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. LtvEGYQSSGsA

Chain	Residue	Details
A	LEU181-ALA192

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Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU184
A	GLU94

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

Chain	Residue	Details
B	GLU184
B	GLU94

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