› 1ppg

X-ray diffraction
2.3Å resolution

The refined 2.3 angstroms crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor

Released:
DOI: 10.2210/pdb1ppg/pdb
PDB entry 1ppg coloured by chain, front view.
PDB entry 1ppg coloured by chain, side view.
PDB entry 1ppg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The refined 2.3 A crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor.
Wei AZ, Mayr I, Bode W
FEBS Lett 234 367-73 (1988)
PMID: 3391280

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

Assemblies composition:
hetero hexamer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140065 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 distinct):
Neutrophil elastase Chain: E
Molecule details ›
Chain: E
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
MEO-SUCCINYL-ALA-ALA-PRO-VAL CHLOROMETHYLKETONE Chain: I
Molecule details ›
Chain: I
Length: 6 amino acids
Theoretical weight: 507 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN, GAL, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC, NDG, GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P63
Unit cell:
a: 74.2Å b: 74.2Å c: 70.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.145 0.145 not available
Expression system: Not provided

Quick links

Citations

10 review citations

Structural basis of substrate specificity in the serine proteases.
Perona et al. (1995)
9 more

5 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
4 more