› 1rxp

X-ray diffraction
1.7Å resolution

STRUCTURE OF TRYPSIN (ORTHORHOMBIC) WITH 1-(4-TERT-BUTYLCARBAMOYL- PIPERAZINE-1-CARBONYL)-3-(3-GUANIDINO-PROPYL)-4-OXO-AZETIDINE-2-CARBOXYLIC ACID

Released:
DOI: 10.2210/pdb1rxp/pdb
PDB entry 1rxp coloured by chain, front view.
PDB entry 1rxp coloured by chain, side view.
PDB entry 1rxp coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Solid-phase synthesis and SAR of 4-carboxy-2-azetidinone mechanism-based tryptase inhibitors.
Sutton JC, Bolton SA, Davis ME, Hartl KS, Jacobson B, Mathur A, Ogletree ML, Slusarchyk WA, Zahler R, Seiler SM, Bisacchi GS
Bioorg Med Chem Lett 14 2233-9 (2004)
PMID: 15081015

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: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
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

3 bound ligands:
Ligand CA 1 x CA
Ligand SO4 1 x SO4
Ligand 169 1 x 169
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 54.29Å b: 58.25Å c: 66.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.222

Quick links

Citations

3 review citations

The chemistry and biological potential of azetidin-2-ones.
Arya et al. (2014)
2 more

1 mention without citation

Placement of molecules in (not out of) the cell.
Dauter Z. (2013)