› 1hny

X-ray diffraction
1.8Å resolution

The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes

Released:
DOI: 10.2210/pdb1hny/pdb
PDB entry 1hny coloured by chain, front view.
PDB entry 1hny coloured by chain, side view.
PDB entry 1hny coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes.
Brayer GD, Luo Y, Withers SG
Protein Sci 4 1730-42 (1995)
PMID: 8528071

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-138163 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pancreatic alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.93 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P04746 (Residues: 16-511; Coverage: 100%)
Gene name: AMY2A
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
Spacegroup: P212121
Unit cell:
a: 53.04Å b: 74.8Å c: 137.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 not available

Quick links

Citations

13 review citations

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

27 mentions without citation

Advanced Bioinformatics Tools in the Pharmacokinetic Profiles of Natural and Synthetic Compounds with Anti-Diabetic Activity.
Udrea et al. (2021)
26 more