› 1v2m

X-ray diffraction
1.65Å resolution

Benzamidine in complex with bovine trypsin variant X(triple.Glu)bT.A1

Released:
DOI: 10.2210/pdb1v2m/pdb
PDB entry 1v2m coloured by chain, front view.
PDB entry 1v2m coloured by chain, side view.
PDB entry 1v2m coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Understanding protein-ligand interactions: the price of protein flexibility.
Rauh D, Klebe G, Stubbs MT
J Mol Biol 335 1325-41 (2004)
PMID: 14729347

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: T
Molecule details ›
Chain: T
Length: 223 amino acids
Theoretical weight: 23.4 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand BEN 1 x BEN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P3121
Unit cell:
a: 54.93Å b: 54.93Å c: 108.41Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.213 0.237
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Determinants of specificity in coagulation proteases.
Page et al. (2005)
28 other articles

1 mention without citation

Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations.
Spraggon et al. (2009)