Brand  (β version)

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Ligands
Code Name Style Show Link
BGC Beta-D-glucopyranose
GLC Alpha-D-glucopyranose
: Polysaccharide
Non-standard Residues
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Glycosylation
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Code : 1B1Y   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : SEVENFOLD MUTANT OF BARLEY BETA-AMYLASE
Release Data : 1998-12-02
Compound :
mol_id molecule chains
1 PROTEIN (BETA-AMYLASE) A
ec: 3.2.1.2
mutation: M185L,S295A,I297V,S350P,S351P,Q352D,A376S
Source :
mol_id organism_scientific expression_system
1 Hordeum vulgare  (taxid:4513) Escherichia coli  (taxid:562)
variant: CV. HARUNA
expression_system_variant: JM 109
expression_system_vector_type: PLASMID
expression_system_plasmid: PB927
Authors : Mikami, B., Yoon, H.J., Yoshigi, N.
Keywords : HYDROLASE(O-GLYCOSYL), HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.5 Å )
Citation :

The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 A resolution.

Mikami, B.,Yoon, H.J.,Yoshigi, N.
(1999)  J.Mol.Biol.  285 : 1235 - 1243

PubMed: 9918723
DOI: 10.1006/jmbi.1998.2379

Construction of a Plasmid Used for the Expression of a Sevenfold-Mutant Barley Beta-Amylase with Increased Thermostability in Escherichia Coli and Properties of the Sevenfold-Mutant Beta-Amylase

Yoshigi, N.,Okada, Y.,Maeba, H.  et al.
(1995)  J.Biochem.(Tokyo)  118 : 562

Chain : A
UniProt : P16098 (AMYB_HORVU)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains. 3.2.1.2 -
-