PDBe 2laa

Solution NMR

Solution Strucuture of the CBM25-1 of beta/alpha-amylase from Paenibacillus polymyxa

Released:
Source organism: Paenibacillus polymyxa
Entry authors: Horibe I, Nishimura S, Takahashi R, Ohkubo T, Yoshida 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:
Biological process:
  • not assigned
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: 104 amino acids
Theoretical weight: 10.75 KDa
Source organism: Paenibacillus polymyxa
Expression system: Escherichia coli
UniProt:
  • Canonical: P21543 (Residues: 455-558; Coverage: 9%)
Sequence domains: Carbohydrate binding domain (family 25)
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 93%
Refinement method: simulated annealing
Chemical shifts: BMR17518  
Expression system: Escherichia coli