› 1e3z

X-ray diffraction
1.93Å resolution

Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A

Released:
DOI: 10.2210/pdb1e3z/pdb
PDB entry 1e3z coloured by chain, front view.
PDB entry 1e3z coloured by chain, side view.
PDB entry 1e3z coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes.
Brzozowski AM, Lawson DM, Turkenburg JP, Bisgaard-Frantzen H, Svendsen A, Borchert TV, Dauter Z, Wilson KS, Davies GJ
Biochemistry 39 9099-107 (2000)
PMID: 10924103

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-132829 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 483 amino acids
Theoretical weight: 55.04 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Bacillus amyloliquefaciens
UniProt:
  • Canonical: P00692 (Residues: 32-514; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, GLD
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, GLD
Carbohydrate polymer
3 bound ligands:
Ligand CA 4 x CA
Ligand NA 1 x NA
Ligand ACI 3 x ACI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2221
Unit cell:
a: 52.72Å b: 78.27Å c: 238.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.13 0.13 0.2
Expression system: Bacillus amyloliquefaciens

Quick links

Citations

4 review citations

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

2 mentions without citation

Structural basis of glycogen branching enzyme deficiency and pharmacologic rescue by rational peptide design.
Froese et al. (2015)
1 more