› 2zeb

X-ray diffraction
2.5Å 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-172371 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptase alpha/beta-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 243 amino acids
Theoretical weight: 27.27 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15661 (Residues: 31-273; Coverage: 95%)
Gene names: TPS1, TPS2, TPSAB1, TPSB1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand 11M 4 x 11M
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P41
Unit cell:
a: 82.67Å b: 82.67Å c: 171.565Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.225
Expression system: Not provided

Quick links

Citations

4 review citations

Mast cell proteases as pharmacological targets.
Caughey GH. (2016)
3 more

2 mentions without citation

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