2XFY

Crystal structure of Barley Beta-Amylase complexed with alpha- cyclodextrin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0016161	molecular_function	beta-amylase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0042802	molecular_function	identical protein binding
A	0102229	molecular_function	amylopectin maltohydrolase activity

Functional Information from PROSITE/UniProt

site_id	PS00506
Number of Residues	9
Details	BETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD

Chain	Residue	Details
A	HIS91-ASP99

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site_id	PS00679
Number of Residues	11
Details	BETA_AMYLASE_2 Beta-amylase active site 2. GpAGEMRYPSY

Chain	Residue	Details
A	GLY180-TYR190

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10050

Chain	Residue	Details
A	GLU184

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P10538

Chain	Residue	Details
A	GLU378

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P10538

Chain	Residue	Details
A	ASP51
A	HIS91
A	ASP99
A	LYS293
A	HIS298
A	THR340
A	ASN379
A	ARG418

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