› 3v7t

X-ray diffraction
2.09Å resolution

Crystal Structure of Human Beta-Tryptase Complexed with a Synthetic Inhibitor with a Tropanylamide Scaffold

Released:
DOI: 10.2210/pdb3v7t/pdb
PDB entry 3v7t coloured by chain, front view.
PDB entry 3v7t coloured by chain, side view.
PDB entry 3v7t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A β-tryptase inhibitor with a tropanylamide scaffold to improve in vitro stability and to lower hERG channel binding affinity.
Liang G, Choi-Sledeski YM, Shum P, Chen X, Poli GB, Kumar V, Minnich A, Wang Q, Tsay J, Sides K, Kang J, Zhang Y
Bioorg Med Chem Lett 22 1606-10 (2012)
PMID: 22264487

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

2 bound ligands:
Ligand 0GX 4 x 0GX
Ligand CO3 2 x CO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P41
Unit cell:
a: 81.719Å b: 81.719Å c: 170.684Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.234
Expression system: Komagataella pastoris

Quick links

Citations

1 review citation

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

1 mention without citation

Allosteric control of βII-tryptase by a redox active disulfide bond.
Cook et al. (2013)