› 2xfy

X-ray diffraction
1.21Å resolution

Crystal structure of Barley Beta-Amylase complexed with alpha- cyclodextrin

Released:
DOI: 10.2210/pdb2xfy/pdb
PDB entry 2xfy coloured by chain, front view.
PDB entry 2xfy coloured by chain, side view.
PDB entry 2xfy 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
Macromolecules (2 distinct):
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

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 68.846Å b: 71.466Å c: 92.472Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.124 0.122 0.153

Quick links

Citations

2 review citations

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

7 mentions without citation

Beta cyclodextrins bind, stabilize, and remove lipofuscin bisretinoids from retinal pigment epithelium.
Nociari et al. (2014)
6 more