1sua

X-ray diffraction
2.1Å resolution

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:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-133534 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin BPN' Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 26.62 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 76%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
TETRAPEPTIDE ALA-LEU-ALA-LEU Chain: C
Molecule details ›
Chain: C
Length: 4 amino acids
Theoretical weight: 386 Da
Source organism: Bacillus amyloliquefaciens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 53.53Å b: 60.33Å c: 83.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 not available
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided