› 1pif

X-ray diffraction
2.3Å resolution

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
Macromolecule:
Pancreatic alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.37 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00690 (Residues: 16-511; Coverage: 100%)
Gene name: AMY2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 70.7Å b: 114.9Å c: 118.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 0.208

Quick links

Citations

4 review citations

Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
MacGregor et al. (2001)
3 more

13 mentions without citation

Cyanidin-3-O-glucoside: Physical-Chemistry, Foodomics and Health Effects.
Olivas-Aguirre et al. (2016)
12 more