› 1amy

X-ray diffraction
2.8Å resolution

CRYSTAL AND MOLECULAR STRUCTURE OF BARLEY ALPHA-AMYLASE

Released:
DOI: 10.2210/pdb1amy/pdb
PDB entry 1amy coloured by chain, front view.
PDB entry 1amy coloured by chain, side view.
PDB entry 1amy coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Crystal and molecular structure of barley alpha-amylase.
Kadziola A, Abe J, Svensson B, Haser R
J Mol Biol 239 104-21 (1994)
PMID: 8196040

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:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137380 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase type B isozyme Chain: A
Molecule details ›
Chain: A
Length: 403 amino acids
Theoretical weight: 44.99 KDa
Source organism: Hordeum vulgare
Expression system: Not provided
UniProt:
  • Canonical: P04063 (Residues: 25-427; Coverage: 100%)
Gene name: AMY1.2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 135.2Å b: 135.2Å c: 79.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.153 0.153 not available
Expression system: Not provided

Quick links

Citations

12 review citations

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

9 mentions without citation

Toward a resolution of the introns early/late debate: only phase zero introns are correlated with the structure of ancient proteins.
de Souza et al. (1998)
8 more