› 4u32

X-ray diffraction
1.65Å resolution

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Kunitz-type protease inhibitor 2 Chain: X
Molecule details ›
Chain: X
Length: 55 amino acids
Theoretical weight: 6.3 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: O43291 (Residues: 34-88; Coverage: 24%)
Gene names: HAI2, KOP, SPINT2
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Trypsin-3 Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 24.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35030 (Residues: 81-304; Coverage: 74%)
Gene names: PRSS3, PRSS4, TRY3, TRY4
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand NAG 1 x NAG
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P212121
Unit cell:
a: 37.194Å b: 70.19Å c: 123.033Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.213
Expression systems:
  • Komagataella pastoris
  • Escherichia coli

Quick links

Citations

1 review citation

The Inter-α-Trypsin Inhibitor Family: Versatile Molecules in Biology and Pathology.
Lord et al. (2020)
15 other articles

5 mentions without citation

TMPRSS2: A potential target for treatment of influenza virus and coronavirus infections.
Shen et al. (2017)
4 more