› 1a0l

X-ray diffraction
3Å resolution

HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE

Released:
DOI: 10.2210/pdb1a0l/pdb
PDB entry 1a0l coloured by chain, front view.
PDB entry 1a0l coloured by chain, side view.
PDB entry 1a0l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore.
Pereira PJ, Bergner A, Macedo-Ribeiro S, Huber R, Matschiner G, Fritz H, Sommerhoff CP, Bode W
Nature 392 306-11 (1998)
PMID: 9521329

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: 244 amino acids
Theoretical weight: 27.39 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P20231 (Residues: 31-274; Coverage: 95%)
Gene names: TPS2, TPSB2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand APA 4 x APA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P41
Unit cell:
a: 82.93Å b: 82.93Å c: 172.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.276

Quick links

Citations

42 review citations

Protease-activated receptors: contribution to physiology and disease.
Ossovskaya et al. (2004)
41 more

7 mentions without citation

Mast cell glycosaminoglycans.
Mulloy et al. (2017)
6 more