PDBe 1utn

X-ray diffraction
1.15Å resolution

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

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cationic trypsin Chain: A
Molecule details ›
Chain: A
Length: 243 amino acids
Theoretical weight: 25.44 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 4-246; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: P212121
Unit cell:
a: 54.15Å b: 56.73Å c: 66.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.113 not available 0.155