PDBe 1ava

X-ray diffraction
1.9Å resolution

AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED

Released:

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-amylase type B isozyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 403 amino acids
Theoretical weight: 44.99 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: P04063 (Residues: 25-427; Coverage: 100%)
Gene name: AMY1.2
Sequence domains:
Structure domains:
Alpha-amylase/subtilisin inhibitor Chains: C, D
Molecule details ›
Chains: C, D
Length: 181 amino acids
Theoretical weight: 19.91 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: P07596 (Residues: 23-203; Coverage: 100%)
Sequence domains: Trypsin and protease inhibitor
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 74.5Å b: 96.18Å c: 170.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.269