› 2fpz

X-ray diffraction
2Å resolution

Human tryptase with 2-amino benzimidazole

Released:
DOI: 10.2210/pdb2fpz/pdb
PDB entry 2fpz coloured by chain, front view.
PDB entry 2fpz coloured by chain, side view.
PDB entry 2fpz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-guided design of peptide-based tryptase inhibitors.
McGrath ME, Sprengeler PA, Hirschbein B, Somoza JR, Lehoux I, Janc JW, Gjerstad E, Graupe M, Estiarte A, Venkataramani C, Liu Y, Yee R, Ho JD, Green MJ, Lee CS, Liu L, Tai V, Spencer J, Sperandio D, Katz BA
Biochemistry 45 5964-73 (2006)
PMID: 16681368

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 270 4 x 270
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P31
Unit cell:
a: 78.895Å b: 78.895Å c: 165.981Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.207 0.24
Expression system: Komagataella pastoris

Quick links

Citations

9 citation in other articles

Purification and characterization of fibrinolytic alkaline protease from Fusarium sp. BLB.
Ueda et al. (2007)
8 more

2 mentions without citation

Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors.
Ribeiro et al. (2010)
1 more