1DHK

STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004556	molecular_function	alpha-amylase activity
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005975	biological_process	carbohydrate metabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016160	molecular_function	amylase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031404	molecular_function	chloride ion binding
A	0043169	molecular_function	cation binding
A	0046872	molecular_function	metal ion binding
B	0015066	molecular_function	alpha-amylase inhibitor activity
B	0030246	molecular_function	carbohydrate binding

Functional Information from PROSITE/UniProt

site_id	PS00307
Number of Residues	7
Details	LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VTVEFDT

Chain	Residue	Details
B	VAL98-THR104

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site_id	PS00308
Number of Residues	10
Details	LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. VYDWVSVGFS

Chain	Residue	Details
B	VAL171-SER180

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10100643

Chain	Residue	Details
B	ASN12
B	ASN65
B	ASN140

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	PHE248

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631

Chain	Residue	Details
A	CYS115
A	ASP173
A	TYR182
A	ASN216

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631

Chain	Residue	Details
A	VAL210
A	GLU352

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LEU313

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P04746

Chain	Residue	Details
A	PHE315

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000250|UniProtKB:P04746

Chain	Residue	Details
A	LEU16

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site_id	SWS_FT_FI8
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine

Chain	Residue	Details
A	ILE427

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
A	ASP300
A	ASP197
A	GLU233

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

Chain	Residue	Details
A	ASP197
A	GLU233

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
A	ASP236
A	ASP197

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