› 1hx0

X-ray diffraction
1.38Å resolution

Structure of pig pancreatic alpha-amylase complexed with the "truncate" acarbose molecule (pseudotrisaccharide)

Released:
DOI: 10.2210/pdb1hx0/pdb
PDB entry 1hx0 coloured by chain, front view.
PDB entry 1hx0 coloured by chain, side view.
PDB entry 1hx0 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex.
Qian M, Nahoum V, Bonicel J, Bischoff H, Henrissat B, Payan F
Biochemistry 40 7700-9 (2001)
PMID: 11412124

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, AC1
Ligand BGC 1 x BGC
Ligand GLC 2 x GLC
Ligand AC1 2 x AC1
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
3 bound ligands:
Ligand CL 4 x CL
Ligand CA 1 x CA
Ligand EDO 12 x EDO
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 69.28Å b: 113.55Å c: 117.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.108 0.108 0.13
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.
Franco et al. (2002)
3 more

13 mentions without citation

Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure-activity relationship.
Proença et al. (2019)
12 more