PDBe 1bag

X-ray diffraction
2.5Å resolution

ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 425 amino acids
Theoretical weight: 47.07 KDa
Source organism: Bacillus subtilis
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P00691 (Residues: 42-466; Coverage: 67%)
Gene names: BSU03040, amyA, amyE
Sequence domains: Alpha amylase, catalytic domain
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 72.59Å b: 74.06Å c: 117.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.252
Expression system: Bacillus subtilis