1xuh

X-ray diffraction
2.2Å resolution

TRYPSIN-KETO-BABIM-CO+2, PH 8.2

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


No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 54.99Å b: 54.99Å c: 109.63Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.135 0.135 0.188