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
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Pullulanase A (preferred)
PDBe Complex ID:
PDB-CPX-101403 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Pullulanase A
Molecule details ›
Chain: A
Length: 1014 amino acids
Theoretical weight: 114.84 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 1014 amino acids
Theoretical weight: 114.84 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A0A0H2UNG0 (Residues: 135-1143; Coverage: 82%)
Sequence domains:
- Bacterial pullanase-associated domain
- Carbohydrate-binding module 48 (Isoamylase N-terminal domain)
- Alpha amylase, catalytic domain
- SpuA C-terminal
Ligands and Environments
Experiments and Validation Details
X-ray source:
RIGAKU MICROMAX-002
Spacegroup:
P212121
Expression system: Escherichia coli BL21(DE3)
