PDBe 1ua3

X-ray diffraction
2.01Å resolution

Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides

Released:
Source organism: Sus scrofa
Primary publication:
Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides.
J. Protein Chem. 22 275-84 (2003)
PMID: 12962327

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pancreatic alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.49 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00690 (Residues: 16-511; Coverage: 100%)
Gene name: AMY2
Sequence domains:
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 69.781Å b: 113.183Å c: 116.924Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.175 0.196