1o2l

X-ray diffraction
1.68Å resolution

Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed 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
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
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
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 63.39Å b: 61.94Å c: 70.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.219