› 1elf

X-ray diffraction
1.7Å resolution

NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH

Released:
DOI: 10.2210/pdb1elf/pdb
PDB entry 1elf coloured by chain, front view.
PDB entry 1elf coloured by chain, side view.
PDB entry 1elf coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function of pH.
Ding X, Rasmussen BF, Demuth HU, Ringe D, Steinmetz AC
Biochemistry 34 7749-56 (1995)
PMID: 7779821

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133451 (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
Expression system: Not provided
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:
Ligand CA 1 x CA
Ligand SO4 2 x SO4
Ligand BAF 1 x BAF
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 52.27Å b: 58.09Å c: 75.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Not provided

Quick links

Citations

2 citation in other articles

Inhibition of dipeptidyl peptidase IV (DPP IV) by 2-(2-amino-1-fluoro-propylidene)-cyclopentanecarbonitrile, a fluoroolefin containing peptidomimetic.
Zhao et al. (2003)
1 more