6XSV

X-ray structure of a tetragonal crystal form of alpha amylase from Aspergillus oryzae (Tala-Amylase) at 1.65 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004556	molecular_function	alpha-amylase activity
A	0005509	molecular_function	calcium ion binding
A	0005975	biological_process	carbohydrate metabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0043169	molecular_function	cation binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:9283074

Chain	Residue	Details
A	ASP206

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:9283074

Chain	Residue	Details
A	GLU230

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305|PubMed:9283074

Chain	Residue	Details
A	HIS122
A	ARG204
A	LYS209
A	GLY234
A	ASP297
A	ARG344
A	GLN35
A	TRP83

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:16880540, ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074

Chain	Residue	Details
A	ASP175
A	HIS210
A	ASN121
A	GLU162

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site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:9283074

Chain	Residue	Details
A	ASP206
A	GLU230

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000305|PubMed:9283074

Chain	Residue	Details
A	ASP297

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site_id	SWS_FT_FI7
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16880540

Chain	Residue	Details
A	ASN197

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