1sib

X-ray diffraction
2.4Å resolution

REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES

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.
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):
Subtilisin BPN' Chain: E
Molecule details ›
Chain: E
Length: 275 amino acids
Theoretical weight: 27.55 KDa
Source organism: Bacillus subtilis
Expression system: Not provided
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 78%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Eglin C Chain: I
Molecule details ›
Chain: I
Length: 70 amino acids
Theoretical weight: 8.07 KDa
Source organism: Hirudo medicinalis
Expression system: Escherichia coli
UniProt:
  • Canonical: P01051 (Residues: 1-70; Coverage: 100%)
Structure domains: Trypsin Inhibitor V, subunit A

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 84.9Å b: 84.9Å c: 89.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 not available not available
Expression systems:
  • Not provided
  • Escherichia coli