› 4a6l

X-ray diffraction
2.05Å resolution

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-, but with more restricted specificity than trypsin.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148879 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptase beta-2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 245 amino acids
Theoretical weight: 27.49 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P20231 (Residues: 31-275; Coverage: 95%)
Gene names: TPS2, TPSB2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand P43 4 x P43
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P41
Unit cell:
a: 82.234Å b: 82.234Å c: 170.654Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.211
Expression system: Komagataella pastoris

Quick links

Citations

1 review citation

Tryptase inhibitors: a patent review.
Ni et al. (2017)
7 other articles

4 mentions without citation

Structural protein-ligand interaction fingerprints (SPLIF) for structure-based virtual screening: method and benchmark study.
Da et al. (2014)
3 more