PDBe 1ton

X-ray diffraction
1.8Å resolution

RAT SUBMAXILLARY GLAND SERINE PROTEASE, TONIN. STRUCTURE SOLUTION AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tonin Chain: A
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 25.69 KDa
Source organism: Rattus rattus
Expression system: Not provided
UniProt:
  • Canonical: P00759 (Residues: 25-259; Coverage: 98%)
Gene names: Klk-2, Klk2, Ton
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 48.58Å b: 48.58Å c: 200.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 not available not available
Expression system: Not provided