2AAA

CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004556	molecular_function	alpha-amylase activity
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0008152	biological_process	metabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 485

Chain	Residue
A	ASP121
A	GLU162
A	ASP175
A	GLU210
A	HOH495
A	HOH499
A	HOH590

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 486

Chain	Residue
A	HOH507
A	HOH599
A	HOH789
A	HOH800
A	HOH801
A	ASP206
A	GLU230

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:2207069

Chain	Residue	Details
A	ASP206

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:2207069

Chain	Residue	Details
A	GLU230

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P0C1B3

Chain	Residue	Details
A	TRP83
A	HIS122
A	ARG204
A	LEU209
A	GLY234
A	ASP297
A	ARG344

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site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:2207069, ECO:0007744|PDB:2AAA

Chain	Residue	Details
A	ASP121
A	GLU162
A	ASP175
A	ASP206
A	GLU210
A	GLU230

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P0C1B3

Chain	Residue	Details
A	ASP297

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site_id	SWS_FT_FI6
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN24
A	ASN157
A	ASN197

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