Function and Biology Details
Reaction catalysed:
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectinand glycogen, and in the alpha- and beta-limit dextrins of amylopectinand glycogen.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Pullulanase (preferred)
PDBe Complex ID:
PDB-CPX-128507 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pullulanase
Molecule details ›
Chain: A
Length: 103 amino acids
Theoretical weight: 12.08 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Bacterial pullanase-associated domain
Structure domains: Immunoglobulin-like
Length: 103 amino acids
Theoretical weight: 12.08 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
O33840 (Residues: 18-120; Coverage: 12%)
Sequence domains: Bacterial pullanase-associated domain
Structure domains: Immunoglobulin-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
Spacegroup:
R32
Expression system: Escherichia coli BL21(DE3)
