PDBe 3bx1

X-ray diffraction
1.85Å resolution

Complex between the Barley alpha-Amylase/Subtilisin Inhibitor and the subtilisin Savinase


Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero octamer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin Savinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 269 amino acids
Theoretical weight: 26.72 KDa
Source organism: Bacillus lentus
Expression system: Bacillus subtilis
  • Canonical: P29600 (Residues: 1-269; Coverage: 100%)
Sequence domains: Subtilase family
Structure domains: Rossmann fold
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
Expression system: Komagataella pastoris
  • 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

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P41212
Unit cell:
a: 100.637Å b: 100.637Å c: 216.242Å
α: 90° β: 90° γ: 90°
R R work R free
0.204 0.202 0.239
Expression systems:
  • Bacillus subtilis
  • Komagataella pastoris