1jrs

X-ray diffraction
1.8Å resolution

HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN

Released:
Source organisms:
Primary publication:
Two crystal structures of the leupeptin-trypsin complex.
Protein Sci. 5 752-8 (1996)
PMID: 8845765

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cationic trypsin Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Leupeptin Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 430 Da
Source organism: Streptomyces roseus
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 63.686Å b: 69.373Å c: 63.013Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.207
Expression system: Not provided