› 3l2l

X-ray diffraction
2.11Å resolution

X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Limit Dextrin and Oligosaccharide

Released:
DOI: 10.2210/pdb3l2l/pdb
PDB entry 3l2l coloured by chain, front view.
PDB entry 3l2l coloured by chain, side view.
PDB entry 3l2l coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
X-ray crystallographic analyses of pig pancreatic alpha-amylase with limit dextrin, oligosaccharide, and alpha-cyclodextrin.
Larson SB, Day JS, McPherson A
Biochemistry 49 3101-15 (2010)
PMID: 20222716

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 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: 55.44 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00690 (Residues: 16-511; Coverage: 100%)
Gene name: AMY2
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
3 bound ligands:
Ligand GLC 1 x GLC
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 RU200
Spacegroup: P212121
Unit cell:
a: 70.59Å b: 114.82Å c: 118.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.119 0.115 0.157

Quick links

Citations

1 review citation

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

3 mentions without citation

Defining structural and evolutionary modules in proteins: a community detection approach to explore sub-domain architecture.
Hleap et al. (2013)
2 more