X-ray diffraction
2Å resolution

Structural analysis of the active site of porcine pancreatic elastase based on the x-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors


Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Chymotrypsin-like elastase family member 1 Chain: E
Molecule details ›
Chain: E
Length: 240 amino acids
Theoretical weight: 25.93 KDa
Source organism: Sus scrofa
Expression system: Not provided
  • Canonical: P00772 (Residues: 27-266; Coverage: 96%)
Gene names: CELA1, ELA1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 52.03Å b: 57.76Å c: 75.319Å
α: 90° β: 90° γ: 90°
R R work R free
0.196 0.196 not available
Expression system: Not provided