› 1ob0

X-ray diffraction
1.83Å resolution

Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface

Released:
DOI: 10.2210/pdb1ob0/pdb
PDB entry 1ob0 coloured by chain, front view.
PDB entry 1ob0 coloured by chain, side view.
PDB entry 1ob0 coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface.
Machius M, Declerck N, Huber R, Wiegand G
J Biol Chem 278 11546-53 (2003)
PMID: 12540849

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: 55.31 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 RU200
Spacegroup: P61
Unit cell:
a: 91.292Å b: 91.292Å c: 137.466Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.147 0.147 0.154
Expression system: Bacillus subtilis

Quick links

Citations

8 review citations

Protein drug stability: a formulation challenge.
Frokjaer et al. (2005)
7 more

4 mentions without citation

Relating destabilizing regions to known functional sites in proteins.
Dessailly et al. (2007)
3 more