1J18

Crystal Structure of a Beta-Amylase from Bacillus cereus var. mycoides Cocrystallized with Maltose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0005976	biological_process	polysaccharide metabolic process
A	0016161	molecular_function	beta-amylase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0046872	molecular_function	metal ion binding
A	0102229	molecular_function	amylopectin maltohydrolase activity
A	2001070	molecular_function	starch binding

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	HIS89-ASP97

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

Chain	Residue	Details
A	GLY168-TYR178

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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, ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294

Chain	Residue	Details
A	GLU172

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294

Chain	Residue	Details
A	GLU367

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294

Chain	Residue	Details
A	ASP49
A	HIS89
A	ASP97
A	LYS287
A	HIS292
A	THR330
A	ARG397

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site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:10353816

Chain	Residue	Details
A	GLU56
A	ASP60
A	GLN61
A	GLU141
A	GLU144
A	ASN368

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1bya

Chain	Residue	Details
A	ASP97
A	GLU172

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