› 4niw

X-ray diffraction
1.31Å resolution

Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) orthorhombic form

Released:
DOI: 10.2210/pdb4niw/pdb
PDB entry 4niw coloured by chain, front view.
PDB entry 4niw coloured by chain, side view.
PDB entry 4niw coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
N-terminal protein modification by substrate-activated reverse proteolysis.
Liebscher S, Schöpfel M, Aumüller T, Sharkhuukhen A, Pech A, Höss E, Parthier C, Jahreis G, Stubbs MT, Bordusa F
Angew Chem Int Ed Engl 53 3024-8 (2014)
PMID: 24520050

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease 1 Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.34 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 54.522Å b: 58.607Å c: 66.831Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.13 0.128 0.155
Expression system: Escherichia coli

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Citations

14 review citations

Natural Occurring and Engineered Enzymes for Peptide Ligation and Cyclization.
Nuijens et al. (2019)
13 more