2e8y

X-ray diffraction
2.11Å resolution

Crystal structure of pullulanase type I from Bacillus subtilis str. 168

Released:
Source organism: Bacillus subtilis
Entry authors: Mikami B, Malle D, Utsumi S, Iwamoto H, Katsuya Y

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111049 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pullulanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 718 amino acids
Theoretical weight: 81.21 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: C0SPA0 (Residues: 1-718; Coverage: 100%)
Gene names: BSU29930, amyX
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 70.562Å b: 127.682Å c: 189.251Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.238
Expression system: Escherichia coli