› 1wo2

X-ray diffraction
2.01Å resolution

Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion

Released:
DOI: 10.2210/pdb1wo2/pdb
PDB entry 1wo2 coloured by chain, front view.
PDB entry 1wo2 coloured by chain, side view.
PDB entry 1wo2 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase.
Qian M, Ajandouz el H, Payan F, Nahoum V
Biochemistry 44 3194-201 (2005)
PMID: 15736930

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-132822 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Pancreatic alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.47 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P00690 (Residues: 16-511; Coverage: 100%)
Gene name: AMY2
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
3 bound ligands:
Ligand CL 1 x CL
Ligand CA 1 x CA
Ligand EDO 6 x EDO
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 70.09Å b: 113.298Å c: 117.221Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 0.184
Expression system: Escherichia coli

Quick links

Citations

12 citation in other articles

Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases.
Cipolla et al. (2012)
11 more