1MVY

Amylosucrase mutant E328Q co-crystallized with maltoheptaose.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0016757	molecular_function	glycosyltransferase activity
A	0047669	molecular_function	amylosucrase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:15023061, ECO:0000305|PubMed:10828446

Chain	Residue	Details
A	ASP286

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:10828446

Chain	Residue	Details
A	GLN328

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000305|PubMed:11467966, ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061

Chain	Residue	Details
A	ASP144
A	HIS187
A	GLN254
A	ARG284
A	HIS392
A	ASP393
A	ARG509

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000250

Chain	Residue	Details
A	ASP444

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Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP286
A	ALA311

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
A	ASP286
A	GLN346

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

Chain	Residue	Details
A	ASP286
A	ASP427
A	GLN346

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

Chain	Residue	Details
A	ASP286
A	GLN328
A	ASP393

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