› 1ppf

X-ray diffraction
1.8Å resolution

X-RAY CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN LEUKOCYTE ELASTASE (PMN ELASTASE) AND THE THIRD DOMAIN OF THE TURKEY OVOMUCOID INHIBITOR

Released:
DOI: 10.2210/pdb1ppf/pdb
PDB entry 1ppf coloured by chain, front view.
PDB entry 1ppf coloured by chain, side view.
PDB entry 1ppf coloured by chain, top view.
Source organisms:
Primary publication:
X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor.
Bode W, Wei AZ, Huber R, Meyer E, Travis J, Neumann S
EMBO J 5 2453-8 (1986)
PMID: 3640709

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140064 (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
Expression system: Not provided
UniProt:
  • Canonical: P08246 (Residues: 30-247; Coverage: 91%)
Gene names: ELA2, ELANE
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Ovomucoid Chain: I
Molecule details ›
Chain: I
Length: 56 amino acids
Theoretical weight: 6.03 KDa
Source organism: Meleagris gallopavo
Expression system: Not provided
UniProt:
  • Canonical: P68390 (Residues: 130-185; Coverage: 30%)
Sequence domains: Kazal-type serine protease inhibitor domain
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 73.05Å b: 72.55Å c: 52.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.166 not available
Expression system: Not provided

Quick links

Citations

20 review citations

Natural protein proteinase inhibitors and their interaction with proteinases.
Bode et al. (1992)
19 more

35 mentions without citation

Protonation and pK changes in protein-ligand binding.
Onufriev et al. (2013)
34 more