› 2uuy

X-ray diffraction
1.15Å resolution

Structure of a tick tryptase inhibitor in complex with bovine trypsin

Released:
DOI: 10.2210/pdb2uuy/pdb
PDB entry 2uuy coloured by chain, front view.
PDB entry 2uuy coloured by chain, side view.
PDB entry 2uuy coloured by chain, top view.
Source organisms:
Primary publication:
A tick protein with a modified Kunitz fold inhibits human tryptase.
Paesen GC, Siebold C, Harlos K, Peacey MF, Nuttall PA, Stuart DI
J Mol Biol 368 1172-86 (2007)
PMID: 17391695

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
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-133354 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1 Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Tryptase inhibitor Chain: B
Molecule details ›
Chain: B
Length: 52 amino acids
Theoretical weight: 5.79 KDa
Source organism: Rhipicephalus appendiculatus
UniProt:
  • Canonical: Q1EG59 (Residues: 45-96; Coverage: 54%)
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 46.949Å b: 67.69Å c: 69.068Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 0.13 0.163

Quick links

Citations

19 review citations

The role of saliva in tick feeding.
Francischetti et al. (2009)
18 more

19 mentions without citation

Protein-protein docking benchmark version 3.0.
Hwang et al. (2008)
18 more