› 1btu

X-ray diffraction
1.6Å resolution

PORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4R)-1-TOLUENESULPHONYL-3-ETHYL-AZETIDIN-2-ONE-4-CARBOXYLIC ACID

Released:
DOI: 10.2210/pdb1btu/pdb
PDB entry 1btu coloured by chain, front view.
PDB entry 1btu coloured by chain, side view.
PDB entry 1btu coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Inhibition of elastase by N-sulfonylaryl beta-lactams: anatomy of a stable acyl-enzyme complex.
Wilmouth RC, Westwood NJ, Anderson K, Brownlee W, Claridge TD, Clifton IJ, Pritchard GJ, Aplin RT, Schofield CJ
Biochemistry 37 17506-13 (1998)
PMID: 9860865

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133451 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chymotrypsin-like elastase family member 1 Chain: A
Molecule details ›
Chain: A
Length: 240 amino acids
Theoretical weight: 25.93 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00772 (Residues: 27-266; Coverage: 96%)
Gene names: CELA1, ELA1
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 2BL 1 x 2BL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 50.57Å b: 57.93Å c: 74.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 not available 0.22

Quick links

Citations

1 review citation

The enzymes of β-lactam biosynthesis.
Hamed et al. (2013)
11 other articles