› 4mpu

X-ray diffraction
1.65Å resolution

Human beta-tryptase co-crystal structure with (6S,8R)-N,N'-bis[3-({4-[3-(aminomethyl)phenyl]piperidin-1-yl}carbonyl)phenyl]-8-hydroxy-6-(1-hydroxycyclobutyl)-5,7-dioxaspiro[3.4]octane-6,8-dicarboxamide

Released:
DOI: 10.2210/pdb4mpu/pdb
PDB entry 4mpu coloured by chain, front view.
PDB entry 4mpu coloured by chain, side view.
PDB entry 4mpu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Target-Directed Self-Assembly of Homodimeric Drugs Against β-Tryptase.
Giardina SF, Werner DS, Pingle M, Foreman KW, Bergstrom DE, Arnold LD, Barany F
ACS Med Chem Lett 9 827-831 (2018)
PMID: 30128075

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172370 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptase alpha/beta-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 245 amino acids
Theoretical weight: 27.49 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
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

4 bound ligands:
Ligand MES 2 x MES
Ligand SO4 4 x SO4
Ligand PG4 2 x PG4
Ligand X2A 1 x X2A
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P3121
Unit cell:
a: 78.157Å b: 78.157Å c: 165.039Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.216
Expression system: Komagataella pastoris

Quick links

Citations

1 mention without citation

Target-Directed Self-Assembly of Homodimeric Drugs Against β-Tryptase.
Giardina et al. (2018)