› 5a0c

X-ray diffraction
2.1Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Neutrophil elastase Chains: A, B
Molecule details ›
Chains: A, B
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

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
3 bound ligands:
Ligand JJV 2 x JJV
Ligand MES 2 x MES
Ligand XPE 1 x XPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P32
Unit cell:
a: 71.517Å b: 71.517Å c: 97.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.163 0.213

Quick links

Citations

10 review citations

Targeting Neutrophils to Treat Acute Respiratory Distress Syndrome in Coronavirus Disease.
Chiang et al. (2020)
9 more

2 mentions without citation

Freezing the Bioactive Conformation to Boost Potency: The Identification of BAY 85-8501, a Selective and Potent Inhibitor of Human Neutrophil Elastase for Pulmonary Diseases.
von Nussbaum et al. (2015)
1 more