1v2j

X-ray diffraction
1.9Å resolution

BENZAMIDINE IN COMPLEX WITH BOVINE TRYPSIN VARIANT X(SSRI)bT.C1

Released:
Source organism: Bos taurus
Primary publication:
Understanding protein-ligand interactions: the price of protein flexibility.
J. Mol. Biol. 335 1325-41 (2004)
PMID: 14729347

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: T
Molecule details ›
Chain: T
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 61.1Å b: 70.34Å c: 64.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.241
Expression system: Escherichia coli