1BYC

CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0005983	biological_process	starch catabolic process
A	0016161	molecular_function	beta-amylase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

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	HIS93-ASP101

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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	GLY182-TYR192

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15178253","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2474529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8011643","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8174545","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15178253","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8011643","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15178253","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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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	GLU186
A	ASP101

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 436

Chain	Residue	Details
A	ASP101	electrostatic stabiliser
A	GLU186	proton shuttle (general acid/base)
A	THR342	electrostatic stabiliser
A	GLU380	proton shuttle (general acid/base)
A	LEU383	steric role

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