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Ligands
Code Name Style Show Link
CA Calcium ion
AF1 4,6-dideoxy-4-{[(1s,4s,5s,6s)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-beta-D-glucopyranose
BGC Beta-D-glucopyranose
DAF 4,6-dideoxy-4-{[(1s,5r,6s)-3-formyl-5,6-dihydroxy-4-oxocyclohex-2-en-1-yl]amino}-alpha-D-xylo-hex-5-enopyranose
: Polysaccharide
Non-standard Residues
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Glycosylation
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Code : 1BG9   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : BARLEY ALPHA-AMYLASE WITH SUBSTRATE ANALOGUE ACARBOSE
Release Data : 1999-06-15
Compound :
mol_id molecule chains synonym
1 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE A ALPHA-AMYLASE, HIGH PI ISOZYME
ec: 3.2.1.1
Source :
mol_id organism_scientific
1 Hordeum vulgare  (taxid:4513)
variant: CULTIVAR MENUET
organ: GERMINATED SEEDS
Authors : Kadziola, A., Haser, R.
Keywords : HYDROLASE, O-GLYCOSYL
Exp. method : X-RAY DIFFRACTION ( 2.8 Å )
Citation :

Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis.

Kadziola, A.,Sogaard, M.,Svensson, B.  et al.
(1998)  J.Mol.Biol.  278 : 205 - 217

PubMed: 9571044
DOI: 10.1006/jmbi.1998.1683

Crystal and Molecular Structure of Barley Alpha-Amylase

Kadziola, A.,Abe, J.I.,Svensson, B.  et al.
(1994)  J.Mol.Biol.  239 : 104

Chain : A
UniProt : P04063 (AMY2_HORVU)
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:P00693
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