1r0r

X-ray diffraction
1.1Å resolution

1.1 Angstrom Resolution Structure of the Complex Between the Protein Inhibitor, OMTKY3, and the Serine Protease, Subtilisin Carlsberg

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

Assembly composition:
hetero 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
UniProt:
  • Canonical: P00780 (Residues: 106-379; Coverage: 78%)
Gene names: apr, subC
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Ovomucoid Chain: I
Molecule details ›
Chain: I
Length: 51 amino acids
Theoretical weight: 5.59 KDa
Source organism: Meleagris gallopavo
UniProt:
  • Canonical: P68390 (Residues: 135-185; Coverage: 28%)
Sequence domains: Kazal-type serine protease inhibitor domain
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 62.329Å b: 70.81Å c: 127.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.158 0.184