1AGM

Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution

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 PDB Data

site_id	SB1
Number of Residues	7
Details	SUBSITE 1 OF THE ACTIVE SITE

Chain	Residue
A	ARG54
A	ASP55
A	LEU177
A	GLU179
A	ARG305
A	GLU400
A	HOH500

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP403-LEU415

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

Chain	Residue	Details
A	THR173-GLY183

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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	ASP176

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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	GLU179

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

Chain	Residue	Details
A	TRP120

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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	ASN171
A	ASN395

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site_id	SWS_FT_FI5
Number of Residues	6
Details	CARBOHYD: O-linked (Man) serine => ECO:0000250

Chain	Residue	Details
A	SER441
A	SER443
A	SER459
A	SER468
A	ALA442
A	ILE469

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site_id	SWS_FT_FI6
Number of Residues	5
Details	CARBOHYD: O-linked (Man) serine

Chain	Residue	Details
A	SER444
A	SER460
A	VAL445
A	ALA454
A	VAL461

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site_id	SWS_FT_FI7
Number of Residues	3
Details	CARBOHYD: O-linked (Man) threonine => ECO:0000250

Chain	Residue	Details
A	THR452
A	THR462
A	THR464

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site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: O-linked (Man) threonine

Chain	Residue	Details
A	SER453
A	VAL463
A	SER465

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site_id	SWS_FT_FI9
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10051, ECO:0000269|PubMed:1970434

Chain	Residue	Details
A	LEU177

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site_id	SWS_FT_FI10
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10051, ECO:0000269|PubMed:1970434

Chain	Residue	Details
A	GLU180

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site_id	SWS_FT_FI11
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	GLY121

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site_id	SWS_FT_FI12
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine

Chain	Residue	Details
A	GLN172
A	GLY396

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 393

Chain	Residue	Details
A	GLY121	transition state stabiliser
A	LEU177	proton shuttle (general acid/base), transition state stabiliser
A	GLU180	proton shuttle (general acid/base)
A	VAL181	activator
A	GLN401	activator

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