› 1qix

X-ray diffraction
1.9Å resolution

Porcine pancreatic elastase complexed with human beta-casomorphin-7

Released:
DOI: 10.2210/pdb1qix/pdb
PDB entry 1qix coloured by chain, front view.
PDB entry 1qix coloured by chain, side view.
PDB entry 1qix coloured by chain, top view.
Source organisms:
Primary publication:
Structure of a specific acyl-enzyme complex formed between beta-casomorphin-7 and porcine pancreatic elastase.
Wilmouth RC, Clifton IJ, Robinson CV, Roach PL, Aplin RT, Westwood NJ, Hajdu J, Schofield CJ
Nat Struct Biol 4 456-62 (1997)
PMID: 9187653

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-133463 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
BETA-CASOMORPHIN-7 Chain: A
Molecule details ›
Chain: A
Length: 7 amino acids
Theoretical weight: 864 Da
Source organism: Homo sapiens
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: RIGAKU
Spacegroup: P212121
Unit cell:
a: 51.282Å b: 58.24Å c: 75.437Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.219
Expression system: Not provided

Quick links

Citations

1 review citation

Sub-Angstrom resolution enzyme X-ray structures: is seeing believing?
Vrielink et al. (2003)
28 other articles

2 mentions without citation

An automated protocol for modelling peptide substrates to proteases.
Ochoa et al. (2020)
1 more