› 2xfr

X-ray diffraction
0.97Å resolution

Crystal structure of barley beta-amylase at atomic resolution

Released:
DOI: 10.2210/pdb2xfr/pdb
PDB entry 2xfr coloured by chain, front view.
PDB entry 2xfr coloured by chain, side view.
PDB entry 2xfr 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

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: 68.83Å b: 71.338Å c: 92.659Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.114 0.113 0.13

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

6 mentions without citation

Biotechnological Processes in Microbial Amylase Production.
Gopinath et al. (2017)
5 more