› 1jrt

X-ray diffraction
1.7Å resolution

HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN

Released:
DOI: 10.2210/pdb1jrt/pdb
PDB entry 1jrt coloured by chain, front view.
PDB entry 1jrt coloured by chain, side view.
PDB entry 1jrt coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Two crystal structures of the leupeptin-trypsin complex.
Kurinov IV, Harrison RW
Protein Sci 5 752-8 (1996)
PMID: 8845765

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133344 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1 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%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
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: Bos taurus

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 55.615Å b: 55.615Å c: 110.51Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.177 0.218

Quick links

Citations

2 review citations

Prokaryote-derived protein inhibitors of peptidases: A sketchy occurrence and mostly unknown function.
Kantyka et al. (2010)
1 more

4 mentions without citation

Relationship of Pax6 activity levels to the extent of eye development in the mouse, Mus musculus.
Favor et al. (2008)
3 more