› 1hvx

X-ray diffraction
2Å resolution

BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE

Released:
DOI: 10.2210/pdb1hvx/pdb
PDB entry 1hvx coloured by chain, front view.
PDB entry 1hvx coloured by chain, side view.
PDB entry 1hvx coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability.
Suvd D, Fujimoto Z, Takase K, Matsumura M, Mizuno H
J Biochem 129 461-8 (2001)
PMID: 11226887

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-138989 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 515 amino acids
Theoretical weight: 58.89 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P06279 (Residues: 35-549; Coverage: 100%)
Gene name: 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: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 53.55Å b: 93.119Å c: 53.275Å
α: 90° β: 109.31° γ: 90°
R-values:
R R work R free
0.154 0.154 0.197
Expression system: Bacillus subtilis

Quick links

Citations

5 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
4 more

7 mentions without citation

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