1HJS

Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0015926	molecular_function	glucosidase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030247	molecular_function	polysaccharide binding
A	0031218	molecular_function	arabinogalactan endo-1,4-beta-galactosidase activity
A	0045490	biological_process	pectin catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0015926	molecular_function	glucosidase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0016998	biological_process	cell wall macromolecule catabolic process
B	0030247	molecular_function	polysaccharide binding
B	0031218	molecular_function	arabinogalactan endo-1,4-beta-galactosidase activity
B	0045490	biological_process	pectin catabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0015926	molecular_function	glucosidase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016998	biological_process	cell wall macromolecule catabolic process
C	0030247	molecular_function	polysaccharide binding
C	0031218	molecular_function	arabinogalactan endo-1,4-beta-galactosidase activity
C	0045490	biological_process	pectin catabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0015926	molecular_function	glucosidase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0016998	biological_process	cell wall macromolecule catabolic process
D	0030247	molecular_function	polysaccharide binding
D	0031218	molecular_function	arabinogalactan endo-1,4-beta-galactosidase activity
D	0045490	biological_process	pectin catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P48841

Chain	Residue	Details
A	GLU135
B	GLU135
C	GLU135
D	GLU135

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site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P48841

Chain	Residue	Details
A	GLU245
B	GLU245
C	GLU245
D	GLU245

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site_id	SWS_FT_FI3
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12761390

Chain	Residue	Details
A	ASN111
B	ASN111
C	ASN111
D	ASN111

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1fhl

Chain	Residue	Details
A	GLU245
A	GLU135
A	ARG45

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site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1fhl

Chain	Residue	Details
B	GLU245
B	GLU135
B	ARG45

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site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1fhl

Chain	Residue	Details
C	GLU245
C	GLU135
C	ARG45

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site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1fhl

Chain	Residue	Details
D	GLU245
D	GLU135
D	ARG45

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