3WWG

Crystal structure of the N-glycan-deficient variant N448A of isopullulanase complexed with isopanose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005576	cellular_component	extracellular region
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0051675	molecular_function	isopullulanase activity
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005576	cellular_component	extracellular region
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0051675	molecular_function	isopullulanase activity
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005576	cellular_component	extracellular region
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0051675	molecular_function	isopullulanase activity
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005576	cellular_component	extracellular region
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0051675	molecular_function	isopullulanase activity

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DLNNGKQITvtDF

Chain	Residue	Details
A	ASP514-PHE526

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	52
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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