4bnr

X-ray diffraction
2Å resolution

Extremely stable complex of crayfish trypsin with bovine trypsin inhibitor

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
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):
Peptidase S1 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 25.07 KDa
Source organism: Astacus leptodactylus
UniProt:
  • Canonical: Q52V24 (Residues: 1-237; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor Chains: I, J
Molecule details ›
Chains: I, J
Length: 100 amino acids
Theoretical weight: 10.92 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00974 (Residues: 1-100; Coverage: 100%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: R3
Unit cell:
a: 138.98Å b: 138.98Å c: 93.37Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.149 0.182