3KL5

Structure Analysis of a Xylanase From Glycosyl Hydrolase Family Thirty: Carbohydrate Ligand Complexes Reveal this Family of Enzymes Unique Mechanism of Substrate Specificity and Recognition

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004348	molecular_function	glucosylceramidase activity
A	0005576	cellular_component	extracellular region
A	0006665	biological_process	sphingolipid metabolic process
A	0033940	molecular_function	glucuronoarabinoxylan endo-1,4-beta-xylanase activity
A	0045493	biological_process	xylan catabolic process
B	0004348	molecular_function	glucosylceramidase activity
B	0005576	cellular_component	extracellular region
B	0006665	biological_process	sphingolipid metabolic process
B	0033940	molecular_function	glucuronoarabinoxylan endo-1,4-beta-xylanase activity
B	0045493	biological_process	xylan catabolic process
C	0004348	molecular_function	glucosylceramidase activity
C	0005576	cellular_component	extracellular region
C	0006665	biological_process	sphingolipid metabolic process
C	0033940	molecular_function	glucuronoarabinoxylan endo-1,4-beta-xylanase activity
C	0045493	biological_process	xylan catabolic process
D	0004348	molecular_function	glucosylceramidase activity
D	0005576	cellular_component	extracellular region
D	0006665	biological_process	sphingolipid metabolic process
D	0033940	molecular_function	glucuronoarabinoxylan endo-1,4-beta-xylanase activity
D	0045493	biological_process	xylan catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21256135","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21256135","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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