1tyn

X-ray diffraction
2Å resolution

ATOMIC STRUCTURE OF THE TRYPSIN-CYCLOTHEONAMIDE A COMPLEX: LESSONS FOR THE DESIGN OF SERINE PROTEASE INHIBITORS

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cationic trypsin Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 71.73Å b: 71.73Å c: 88.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.169 0.222
Expression system: Not provided