1Q6G

Crystal Structure of Soybean Beta-Amylase Mutant (N340T) with Increased pH Optimum

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

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	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10050, ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:2474529, ECO:0000269|PubMed:8011643, ECO:0000269|PubMed:8174545

Chain	Residue	Details
A	GLU186

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:8011643

Chain	Residue	Details
A	GLU380

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:15178253

Chain	Residue	Details
A	ASP53
A	HIS93
A	ASP101
A	LYS295
A	HIS300
A	THR342
A	ASN381
A	ARG420

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000269|PubMed:2430952

Chain	Residue	Details
A	ALA1

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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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