PDBe 2rg3

X-ray diffraction
1.8Å resolution

Covalent complex structure of elastase

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neutrophil elastase Chain: A
Molecule details ›
Chain: A
Length: 218 amino acids
Theoretical weight: 23.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08246 (Residues: 30-247; Coverage: 91%)
Gene names: ELA2, ELANE
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P63
Unit cell:
a: 73.2Å b: 73.2Å c: 70.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.2 not available
Expression system: Escherichia coli