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X-ray diffraction
1.9Å resolution

Trypsin inhibitors with rigid tripeptidyl aldehydes

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: 237 amino acids
Theoretical weight: 24.74 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 10-246; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 63.67Å b: 63.2Å c: 69.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.157 not available