› 2za5

X-ray diffraction
2.3Å 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 domain:

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 2FF 4 x 2FF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P41
Unit cell:
a: 82.678Å b: 82.678Å c: 170.284Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.233
Expression system: Komagataella pastoris

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Citations

4 review citations

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