1mcv

X-ray diffraction
1.8Å resolution

Crystal Structure Analysis of a Hybrid Squash Inhibitor in Complex with Porcine Pancreatic Elastase

Released:
Source organism: Sus scrofa

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
HEI-TOE I Chain: I
Molecule details ›
Chain: I
Length: 28 amino acids
Theoretical weight: 2.97 KDa
Source organism: Sus scrofa
Expression system: Not provided

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 56.33Å b: 56.44Å c: 72.76Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.221
Expression system: Not provided