PDBe 3dhu

X-ray diffraction
2Å resolution

Crystal structure of an alpha-amylase from Lactobacillus plantarum

Released:
Source organism: Lactobacillus plantarum
Entry authors: Bonanno JB, Dickey M, Bain KT, Iizuka M, Ozyurt S, Smith D, Wasserman S, Sauder JM, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase, maltodextrins and cyclomaltodextrins Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 449 amino acids
Theoretical weight: 51.11 KDa
Source organism: Lactobacillus plantarum
Expression system: Escherichia coli
UniProt:
  • Canonical: F9USZ1 (Residues: 3-440; Coverage: 100%)
Gene names: lp_0179, malS
Sequence domains: Alpha amylase, catalytic domain
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: C2
Unit cell:
a: 202.279Å b: 63.773Å c: 155.677Å
α: 90° β: 102.93° γ: 90°
R-values:
R R work R free
0.203 0.2 0.251
Expression system: Escherichia coli