› 1utl

X-ray diffraction
1.7Å resolution

Trypsin specificity as elucidated by LIE calculations, X-ray structures and association constant measurements

Released:
DOI: 10.2210/pdb1utl/pdb
PDB entry 1utl coloured by chain, front view.
PDB entry 1utl coloured by chain, side view.
PDB entry 1utl coloured by chain, top view.
Source organism: Salmo salar
Primary publication:
Trypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurements.
Leiros HK, Brandsdal BO, Andersen OA, Os V, Leiros I, Helland R, Otlewski J, Willassen NP, Smalås AO
Protein Sci 13 1056-70 (2004)
PMID: 15044735

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152775 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypsin-1 Chain: M
Molecule details ›
Chain: M
Length: 242 amino acids
Theoretical weight: 26 KDa
Source organism: Salmo salar
UniProt:
  • Canonical: P35031 (Residues: 1-242; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
Ligand PRA 1 x PRA
Ligand CA 1 x CA
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: P212121
Unit cell:
a: 44.944Å b: 48.269Å c: 83.102Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.216

Quick links

Citations

1 review citation

Smart micro/nanoparticles in stimulus-responsive drug/gene delivery systems.
Karimi et al. (2016)
38 other articles

1 mention without citation

Fish trypsins: potential applications in biomedicine and prospects for production.
Jesús-de la Cruz et al. (2018)