2sec

X-ray diffraction
1.8Å resolution

STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO

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:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin Carlsberg Chain: E
Molecule details ›
Chain: E
Length: 274 amino acids
Theoretical weight: 27.31 KDa
Source organism: Bacillus licheniformis
Expression system: Not provided
UniProt:
  • Canonical: P00780 (Residues: 106-379; Coverage: 78%)
Gene names: apr, subC
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Eglin C Chain: I
Molecule details ›
Chain: I
Length: 70 amino acids
Theoretical weight: 8.1 KDa
Source organism: Hirudo medicinalis
Expression system: unidentified
UniProt:
  • Canonical: P01051 (Residues: 1-70; Coverage: 100%)
Sequence domains: Potato inhibitor I family
Structure domains: Trypsin Inhibitor V, subunit A

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 38.31Å b: 41.41Å c: 56.5Å
α: 69.51° β: 83.67° γ: 75.32°
R-values:
R R work R free
0.136 not available not available
Expression systems:
  • Not provided
  • unidentified