7O0E

Crystal structure of GH30 (mutant E188A) complexed with aldotriuronic acid from Thermothelomyces thermophila.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004348	molecular_function	glucosylceramidase activity
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005576	cellular_component	extracellular region
A	0006665	biological_process	sphingolipid metabolic process
A	0006680	biological_process	glucosylceramide catabolic process
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
G	0004348	molecular_function	glucosylceramidase activity
G	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
G	0005576	cellular_component	extracellular region
G	0006665	biological_process	sphingolipid metabolic process
G	0006680	biological_process	glucosylceramide catabolic process
G	0016020	cellular_component	membrane
G	0016787	molecular_function	hydrolase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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