› 5wi6

X-ray diffraction
2.72Å resolution

Human beta-1 tryptase mutant Ile99Cys

Released:
DOI: 10.2210/pdb5wi6/pdb
PDB entry 5wi6 coloured by chain, front view.
PDB entry 5wi6 coloured by chain, side view.
PDB entry 5wi6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Dual functionality of β-tryptase protomers as both proteases and cofactors in the active tetramer.
Maun HR, Liu PS, Franke Y, Eigenbrot C, Forrest WF, Schwartz LB, Lazarus RA
J Biol Chem 293 9614-9628 (2018)
PMID: 29661938

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: 245 amino acids
Theoretical weight: 27.47 KDa
Source organism: Homo sapiens
Expression system: Spodoptera
UniProt:
  • Canonical: Q15661 (Residues: 31-275; Coverage: 95%)
Gene names: TPS1, TPS2, TPSAB1, TPSB1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand SO4 7 x SO4
Ligand 0GJ 4 x 0GJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3221
Unit cell:
a: 96.743Å b: 96.743Å c: 238.553Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.193 0.227
Expression system: Spodoptera

Quick links

Citations

2 review citations

Genetic Regulation of Tryptase Production and Clinical Impact: Hereditary Alpha Tryptasemia, Mastocytosis and Beyond.
Sprinzl et al. (2021)
1 more

1 mention without citation

Dual functionality of β-tryptase protomers as both proteases and cofactors in the active tetramer.
Maun et al. (2018)