› 1hj8

X-ray diffraction
1Å resolution

1.00 AA Trypsin from Atlantic Salmon

Released:
DOI: 10.2210/pdb1hj8/pdb
PDB entry 1hj8 coloured by chain, front view.
PDB entry 1hj8 coloured by chain, side view.
PDB entry 1hj8 coloured by chain, top view.
Source organism: Salmo salar
Primary publication:
Atomic resolution structures of trypsin provide insight into structural radiation damage.
Leiros HK, McSweeney SM, Smalås AO
Acta Crystallogr D Biol Crystallogr 57 488-97 (2001)
PMID: 11264577

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
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: A
Molecule details ›
Chain: A
Length: 222 amino acids
Theoretical weight: 23.84 KDa
Source organism: Salmo salar
UniProt:
  • Canonical: P35031 (Residues: 21-242; Coverage: 98%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
Ligand BEN 2 x BEN
Ligand SO4 1 x SO4
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21212
Unit cell:
a: 72.63Å b: 82.77Å c: 30.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.119 not available 0.149

Quick links

Citations

25 citation in other articles

The catalytic pathway of horseradish peroxidase at high resolution.
Berglund et al. (2002)
24 more

9 mentions without citation

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