› 6est

X-ray diffraction
1.8Å resolution

INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3(TFLA) WITH PORCINE PANCREATIC ELASTASE. X-RAY STUDIES AT 1.8 ANGSTROMS

Released:
DOI: 10.2210/pdb6est/pdb
PDB entry 6est coloured by chain, front view.
PDB entry 6est coloured by chain, side view.
PDB entry 6est coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Interaction of the peptide CF3-Leu-Ala-NH-C6H4-CF3 (TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 A.
Li de la Sierra I, Papamichael E, Sakarellos C, Dimicoli JL, Prangé T
J Mol Recognit 3 36-44 (1990)
PMID: 2354062

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
Expression system: Not provided
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 DMF 3 x DMF
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 51.48Å b: 57.98Å c: 75.14Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 not available
Expression system: Not provided

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Citations

1 review citation

Synthetic inhibitors of elastase.
Edwards et al. (1994)
11 other articles