PDBe 3voc

X-ray diffraction
1.95Å resolution

Crystal structure of the catalytic domain of beta-amylase from paenibacillus polymyxa

Released:
Source organism: Paenibacillus polymyxa
Entry authors: Nishimura S, Fujioka T, Nakaniwa T, Tada T

Function and Biology Details

Reactions 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. 
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta/alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 419 amino acids
Theoretical weight: 45.85 KDa
Source organism: Paenibacillus polymyxa
Expression system: Escherichia coli
UniProt:
  • Canonical: P21543 (Residues: 36-454; Coverage: 36%)
Sequence domains: Glycosyl hydrolase family 14
Structure domains: Glycosidases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 61.028Å b: 68.519Å c: 93.904Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.19
Expression system: Escherichia coli