› 2laa

Solution NMR

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

Released:
DOI: 10.2210/pdb2laa/pdb
PDB entry 2laa coloured by chain, ensemble of 20 models, front view.
PDB entry 2laa coloured by chain, ensemble of 20 models, side view.
PDB entry 2laa coloured by chain, ensemble of 20 models, top view.
Source organism: Paenibacillus polymyxa
Entry authors: Horibe I, Nishimura S, Takahashi R, Ohkubo T, Yoshida T

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149287 (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
Expression system: Escherichia coli

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