1nes

X-ray diffraction
1.65Å resolution

STRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTION

Released:

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 trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
UniProt:
  • Canonical: P00772 (Residues: 27-266; Coverage: 96%)
Gene names: CELA1, ELA1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
ACETYL-ALA-PRO-ALA Chains: I, J
Molecule details ›
Chains: I, J
Length: 4 amino acids
Theoretical weight: 283 Da
Source organism: Sus scrofa
Expression system: Not provided

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 51.4Å b: 58.2Å c: 75.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 not available
Expression system: Not provided