› 1bli

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
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:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138987 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 483 amino acids
Theoretical weight: 55.27 KDa
Source organism: Bacillus licheniformis
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P06278 (Residues: 30-512; Coverage: 100%)
Gene names: amyL, amyS
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 3 x CA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P61
Unit cell:
a: 91.3Å b: 91.3Å c: 137.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.154 0.154 0.185
Expression system: Bacillus subtilis

Quick links

Citations

12 review citations

Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
MacGregor et al. (2001)
11 more

24 mentions without citation

Structural and functional adaptation in extremophilic microbial α-amylases.
Ahmad et al. (2022)
23 more