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Ligands
Code Name Style Show Link
CA Calcium ion
BGC Beta-D-glucopyranose
GLC Alpha-D-glucopyranose
: Polysaccharide
Non-standard Residues
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Glycosylation
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Code : 1BAG   PDBj   RCSB PDB   PDBe
Header : ALPHA-AMYLASE
Title : ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE
Release Data : 1998-10-21
Compound :
mol_id molecule chains synonym
1 ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE A ALPHA-AMYLASE
ec: 3.2.1.1
mutation: E208Q
other_details: COMPLEXED WITH MALTOPENTAOSE
Source :
mol_id organism_scientific expression_system
1 Bacillus subtilis  (taxid:1423) Bacillus subtilis  (taxid:1423)
gene: AMY
expression_system_strain: 207-25
expression_system_vector_type: PLASMID
expression_system_vector: PUB110
expression_system_plasmid: PTUB111
expression_system_gene: AMY
Authors : Fujimoto, Z., Mizuno, H., Takase, K., Doui, N.
Keywords : ALPHA-AMYLASE, BACILLUS SUBTILIS, MALTOPENTAOSE, CATALYTIC-SITE MUTANT
Exp. method : X-RAY DIFFRACTION ( 2.5 Å )
Citation :

Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose.

Fujimoto, Z.,Takase, K.,Doui, N.  et al.
(1998)  J.Mol.Biol.  277 : 393 - 407

PubMed: 9514750
DOI: 10.1006/jmbi.1997.1599

Crystallization and Preliminary X-Ray Studies of Wild Type and Catalytic-Site Mutant Alpha-Amylase from Bacillus Subtilis

Mizuno, H.,Morimoto, Y.,Tsukihara, T.  et al.
(1993)  J.Mol.Biol.  234 : 1282

Site-Directed Mutagenesis of Active Site Residues in Bacillus Subtilis Alpha-Amylase

Takase, K.,Matsumoto, T.,Mizuno, H.  et al.
(1992)  Biochim.Biophys.Acta  1120 : 281

Changes in the Properties and Molecular Weights of Bacillus Subtilis M-Type and N-Type Alpha-Amylases Resulting from a Spontaneous Deletion

Yamane, K.,Hirata, Y.,Furusato, T.  et al.
(1984)  J.Biochem.(Tokyo)  96 : 1849

Chain : A
UniProt : P00691 (AMY_BACSU)
Reaction: EC: Evidence:
Physiological Direction:
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D- glucose units. 3.2.1.1 UniProtKB:P06278
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