PDBe 1y3c

X-ray diffraction
1.69Å resolution

Crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 R62A mutant

Released:

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.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin BPN' Chain: E
Molecule details ›
Chain: E
Length: 281 amino acids
Theoretical weight: 28.38 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 78%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Chymotrypsin inhibitor 2 Chain: I
Molecule details ›
Chain: I
Length: 64 amino acids
Theoretical weight: 7.2 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q40059 (Residues: 21-84; Coverage: 76%)
Gene name: Ica-2
Sequence domains: Potato inhibitor I family
Structure domains: Trypsin Inhibitor V, subunit A

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P6522
Unit cell:
a: 93.873Å b: 93.873Å c: 185.065Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.149 0.148 0.178
Expression systems:
  • Bacillus subtilis
  • Escherichia coli BL21(DE3)