Brand  (β version)

PDB ID: 2XGI

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Ligands
Code Name Style Show Link
EDO 1,2-ethanediol PoSSuM
EBQ (3s)-3-hydroxybutyl alpha-D-glucopyranoside PoSSuM
J5B (3r)-3-hydroxybutyl alpha-D-glucopyranoside PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 2XGI   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of Barley Beta-Amylase complexed with 3,4- epoxybutyl alpha-D-glucopyranoside
Release Data : 2010-12-01
Compound :
mol_id molecule chains synonym
1 BETA-AMYLASE A 1,4-ALPHA-D-GLUCAN MALTOHYDROLASE
ec: 3.2.1.2
Source :
mol_id organism_scientific
1 HORDEUM VULGARE  (taxid:4513)
tissue: GRAIN ENDOSPERM
other_details: PROTEIN PURCHASED FROM MEGAZYME
Authors : Rejzek, M., Stevenson, C.E.M., Southard, A.M., Stanley, D., Denyer, K., Smith, A.M., Naldrett, M.J., Lawson, D.M., Field, R.A.
Keywords : GLYCOSIDASE, CARBOHYDRATE METABOLISM, GLYCOSYL HYDROLASE FAMILY 14, STARCH DEGRADATION, GERMINATION, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.30 Å )
Citation :

Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley beta-amylase.

Rejzek, M.,Stevenson, C.E.,Southard, A.M.  et al.
(2011)  Mol Biosyst  7 : 718 - 730

PubMed: 21085740
DOI: 10.1039/c0mb00204f

Reaction

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 -
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