1l0z

X-ray diffraction
1.5Å resolution

THE STRUCTURE OF PORCINE PANCREATIC ELASTASE COMPLEXED WITH XENON AND BROMIDE, CRYOPROTECTED WITH DRY PARAFFIN OIL

Released:
Source organism: Sus scrofa
Primary publication:
Xenon derivatization of halide-soaked protein crystals.
Acta Crystallogr. D Biol. Crystallogr. 58 1413-20 (2002)
PMID: 12198297

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
Macromolecule:
Chymotrypsin-like elastase family member 1 Chain: A
Molecule details ›
Chain: A
Length: 240 amino acids
Theoretical weight: 25.93 KDa
Source organism: Sus scrofa
UniProt:
  • 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
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P212121
Unit cell:
a: 49.5Å b: 57.7Å c: 73.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.166 0.209