› 2xgb

X-ray diffraction
1.2Å resolution

Crystal structure of Barley Beta-Amylase complexed with 2,3- epoxypropyl-alpha-D-glucopyranoside

Released:
DOI: 10.2210/pdb2xgb/pdb
PDB entry 2xgb coloured by chain, front view.
PDB entry 2xgb coloured by chain, side view.
PDB entry 2xgb coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley β-amylase.
Rejzek M, Stevenson CE, Southard AM, Stanley D, Denyer K, Smith AM, Naldrett MJ, Lawson DM, Field RA
Mol Biosyst 7 718-30 (2011)
PMID: 21085740

Function and Biology Details

Reaction catalysed: 
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
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147608 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-amylase Chain: A
Molecule details ›
Chain: A
Length: 535 amino acids
Theoretical weight: 59.67 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: P16098 (Residues: 1-535; Coverage: 100%)
Gene names: AMYB, BMY1
Sequence domains: Glycosyl hydrolase family 14
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
Ligand EPG 1 x EPG
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P212121
Unit cell:
a: 68.622Å b: 71.068Å c: 92.309Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.118 0.117 0.141

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Citations

2 review citations

A broader view: microbial enzymes and their relevance in industries, medicine, and beyond.
Gurung et al. (2013)
1 more