› 3q77

X-ray diffraction
2Å resolution

Structure of human neutrophil elastase in complex with a dihydropyrimidone inhibitor

Released:
DOI: 10.2210/pdb3q77/pdb
PDB entry 3q77 coloured by chain, front view.
PDB entry 3q77 coloured by chain, side view.
PDB entry 3q77 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Unexpected active-site flexibility in the structure of human neutrophil elastase in complex with a new dihydropyrimidone inhibitor.
Hansen G, Gielen-Haertwig H, Reinemer P, Schomburg D, Harrenga A, Niefind K
J Mol Biol 409 681-91 (2011)
PMID: 21549129

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 (2 distinct):
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

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand 2HY 1 x 2HY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P63
Unit cell:
a: 73.732Å b: 73.732Å c: 70.658Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.161 0.159 0.203

Quick links

Citations

7 review citations

Role of Proteases in Chronic Obstructive Pulmonary Disease.
Pandey et al. (2017)
6 more

5 mentions without citation

Paucimannose-Rich N-glycosylation of Spatiotemporally Regulated Human Neutrophil Elastase Modulates Its Immune Functions.
Loke et al. (2017)
4 more