› 1ppi

X-ray diffraction
2.2Å resolution

THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1ppi/pdb
PDB entry 1ppi coloured by chain, front view.
PDB entry 1ppi coloured by chain, side view.
PDB entry 1ppi coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution.
Qian M, Haser R, Buisson G, Duée E, Payan F
Biochemistry 33 6284-94 (1994)
PMID: 8193143

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: 55.44 KDa
Source organism: Sus scrofa
Expression system: Not provided
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: BGC, DAF
Ligand BGC 1 x BGC
Ligand DAF 1 x DAF
2 bound ligands:
Ligand CL 1 x CL
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 56.3Å b: 87.8Å c: 103.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.153 not available
Expression system: Not provided

Quick links

Citations

16 review citations

Mechanisms of enzymatic glycoside hydrolysis.
McCarter et al. (1994)
15 more

22 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
21 more