1AYX

CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA AT 1.7 ANGSTROMS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0000324	cellular_component	fungal-type vacuole
A	0004339	molecular_function	glucan 1,4-alpha-glucosidase activity
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0005976	biological_process	polysaccharide metabolic process
A	0008152	biological_process	metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS A 493

Chain	Residue
A	HOH575
A	TYR63
A	TRP67
A	ARG69
A	ASP70
A	GLU210
A	TRP362
A	LEU471

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site_id	NUL
Number of Residues	2
Details	ENZYME ACTIVE SITE AND TWO CATALYTIC CARBOXYLATES.

Chain	Residue
A	GLU210
A	GLU456

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Functional Information from PROSITE/UniProt

site_id	PS00820
Number of Residues	11
Details	GLUCOAMYLASE Glucoamylase active site region signature. TGf.DlWEEnqG

Chain	Residue	Details
A	THR204-GLY214

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10051

Chain	Residue	Details
A	ASP207

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10051

Chain	Residue	Details
A	GLU210

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	TRP139

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site_id	SWS_FT_FI4
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN88
A	ASN100
A	ASN178

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