› 3bh4

X-ray diffraction
1.4Å resolution

High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase

Released:
DOI: 10.2210/pdb3bh4/pdb
PDB entry 3bh4 coloured by chain, front view.
PDB entry 3bh4 coloured by chain, side view.
PDB entry 3bh4 coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability.
Alikhajeh J, Khajeh K, Ranjbar B, Naderi-Manesh H, Lin YH, Liu E, Guan HH, Hsieh YC, Chuankhayan P, Huang YC, Jeyaraman J, Liu MY, Chen CJ
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 121-9 (2010)
PMID: 20124706

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132829 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 483 amino acids
Theoretical weight: 54.9 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Not provided
UniProt:
  • Canonical: P00692 (Residues: 32-514; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 8 x CA
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21212
Unit cell:
a: 89.76Å b: 148.676Å c: 76.197Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.219
Expression system: Not provided

Quick links

Citations

3 review citations

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

2 mentions without citation

Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability.
Alikhajeh et al. (2010)
1 more