6TOY

Crystal structure of Bacillus paralicheniformis wild-type alpha-amylase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004556	molecular_function	alpha-amylase activity
A	0005509	molecular_function	calcium ion binding
A	0005615	cellular_component	extracellular space
A	0005975	biological_process	carbohydrate metabolic process
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	5
Details	binding site for residue CA A 501

Chain	Residue
A	ASN104
A	ASP194
A	ASP200
A	HIS235
A	HOH805

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site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 502

Chain	Residue
A	ASP204
A	HOH878
A	ASP161
A	ALA181
A	ASP183
A	ASP202

---

site_id	AC3
Number of Residues	5
Details	binding site for residue NA A 503

Chain	Residue
A	ASP161
A	ASP183
A	ASP194
A	ASP200
A	ILE201

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site_id	AC4
Number of Residues	5
Details	binding site for residue NA A 504

Chain	Residue
A	GLY300
A	TYR302
A	HIS406
A	ASN407
A	ASP430

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site_id	AC5
Number of Residues	6
Details	binding site for residue MLI A 505

Chain	Residue
A	ALA232
A	LYS234
A	HIS235
A	GLU261
A	HOH611
A	HOH675

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site_id	AC6
Number of Residues	6
Details	binding site for residue FMT A 506

Chain	Residue
A	ASP164
A	LEU171
A	ASN172
A	MET197
A	TYR198
A	HOH603

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site_id	AC7
Number of Residues	3
Details	binding site for residue ACY A 507

Chain	Residue
A	TYR114
A	ARG134
A	HOH620

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site_id	AC8
Number of Residues	3
Details	binding site for residue ACY A 508

Chain	Residue
A	ARG437
A	ASN463
A	TRP467

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site_id	AC9
Number of Residues	4
Details	binding site for residue ACY A 509

Chain	Residue
A	ARG214
A	THR217
A	HIS247
A	LYS251

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