› 1btp

X-ray diffraction
2.2Å resolution

UNIQUE BINDING OF A NOVEL SYNTHETIC INHIBITOR, N-[3-[4-[4-(AMIDINOPHENOXY)-CARBONYL]PHENYL]-2-METHYL-2-PROPENOYL]-N-ALLYLGLYCINE METHANESULFONATE TO BOVINE TRYPSIN, REVEALED BY THE CRYSTAL STRUCTURE OF THE COMPLEX

Released:
DOI: 10.2210/pdb1btp/pdb
PDB entry 1btp coloured by chain, front view.
PDB entry 1btp coloured by chain, side view.
PDB entry 1btp coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Unique binding of a novel synthetic inhibitor, N-[3-[4-[4-(amidinophenoxy)carbonyl]phenyl]-2-methyl-2-propenoyl]- N-allylglycine methanesulfonate, to bovine trypsin, revealed by the crystal structure of the complex.
Odagaki Y, Nakai H, Senokuchi K, Kawamura M, Hamanaka N, Nakamura M, Tomoo K, Ishida T
Biochemistry 34 12849-53 (1995)
PMID: 7548040

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease 1 Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 24.01 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 18-246; Coverage: 100%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 63.74Å b: 63.08Å c: 69.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available

Quick links

Citations

1 review citation

[Overview of structural study on conformations and intermolecular interactions of biomolecules].
Ishida T. (2012)
3 other articles

3 mentions without citation

Protein-protein docking benchmark version 3.0.
Hwang et al. (2008)
2 more