3EQA

Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004339	molecular_function	glucan 1,4-alpha-glucosidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0005976	biological_process	polysaccharide metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00820
Number of Residues	11
Details	GLUCOAMYLASE Glucoamylase active site region signature. TGy.DlWEEvnG

Chain	Residue	Details
A	THR197-GLY207

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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	ASP200

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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	GLU203

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

Chain	Residue	Details
A	TRP144

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250

Chain	Residue	Details
A	ASN195
A	ASN419

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site_id	SWS_FT_FI5
Number of Residues	8
Details	CARBOHYD: O-linked (Man) serine => ECO:0000269|Ref.4

Chain	Residue	Details
A	SER465
A	SER467
A	SER468
A	SER477
A	SER483
A	SER484
A	SER489
A	SER492

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site_id	SWS_FT_FI6
Number of Residues	3
Details	CARBOHYD: O-linked (Man) threonine => ECO:0000269|Ref.4

Chain	Residue	Details
A	THR476
A	THR486
A	THR488

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1agm

Chain	Residue	Details
A	GLU203
A	GLU424

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