› 1h9l

X-ray diffraction
1.67Å resolution

PORCINE PANCREATIC ELASTASE COMPLEXED WITH ACETYL-VAL-GLU-PRO-ILE-COOH

Released:
DOI: 10.2210/pdb1h9l/pdb
PDB entry 1h9l coloured by chain, front view.
PDB entry 1h9l coloured by chain, side view.
PDB entry 1h9l coloured by chain, top view.
Source organisms:
Primary publication:
Kinetic and crystallographic analysis of complexes formed between elastase and peptides from beta-casein.
Wright PA, Wilmouth RC, Clifton IJ, Schofield CJ
Eur J Biochem 268 2969-74 (2001)
PMID: 11358514

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133457 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
PEPTIDE INHIBITOR Chain: A
Molecule details ›
Chain: A
Length: 5 amino acids
Theoretical weight: 483 Da
Source organism: synthetic construct
Expression system: Not provided
Chymotrypsin-like elastase family member 1 Chain: B
Molecule details ›
Chain: B
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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 50.16Å b: 57.84Å c: 74.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.158 0.199
Expression system: Not provided

Quick links

Citations

5 citation in other articles

Binding structure of elastase inhibitor scyptolin A.
Matern et al. (2003)
4 more

1 mention without citation

Elastin is heterogeneously cross-linked.
Schräder et al. (2018)