PDBe 5a8x

X-ray diffraction
2.23Å resolution

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: 23.32 KDa
Source organism: Homo sapiens
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:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P63
Unit cell:
a: 73.795Å b: 73.795Å c: 70.01Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.174 0.223