› 1ava

X-ray diffraction
1.9Å resolution

AMY2/BASI PROTEIN-PROTEIN COMPLEX FROM BARLEY SEED

Released:
DOI: 10.2210/pdb1ava/pdb
PDB entry 1ava coloured by chain, front view.
PDB entry 1ava coloured by chain, side view.
PDB entry 1ava coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution.
Vallée F, Kadziola A, Bourne Y, Juy M, Rodenburg KW, Svensson B, Haser R
Structure 6 649-59 (1998)
PMID: 9634702

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137381 (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:
Ligand CA 8 x CA
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

Quick links

Citations

6 review citations

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

14 mentions without citation

Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19.
Kozakov et al. (2010)
13 more