› 1b0f

X-ray diffraction
3Å 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 domain:

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: 23.23 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
1 bound ligand:
Ligand SEI 1 x SEI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P4322
Unit cell:
a: 75.8Å b: 75.8Å c: 108.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.16 not available

Quick links

Citations

3 review citations

Docking screens: right for the right reasons?
Kolb et al. (2009)
2 more

9 mentions without citation

ANTIAGE-DB: A Database and Server for the Prediction of Anti-Aging Compounds Targeting Elastase, Hyaluronidase, and Tyrosinase.
Papaemmanouil et al. (2022)
8 more