1ELB: Analogous Inhibitors Of Elastase Do Not Always Bind Analogously

It has been assumed that the structure of a single inhibitor complex is sufficient to define the available subsites of an enzyme that has a unique binding site and a uniquely defined mode for ligand binding--the specificity for these subsites can thus be probed by kinetic experiments. Elastase is an enzyme for which these traditional assumptions, which underlie such structural and kinetic studies, do not hold. Three new crystal structures of elastase complexed to chemically similar inhibitors with similar binding affinities reveal a diversity of binding modes as well as two new subsites on elastase. The existence of multiple binding sites and different binding modes for such similar inhibitors indicates that researchers must proceed with caution when using kinetics to map out protein subsites.
PDB ID: 1ELBDownload
MMDB ID: 102921
PDB Deposition Date: 1993/12/7
Updated in MMDB: 2012/09
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 1ELB: monomeric; determined by author
Molecular Components in 1ELB
Label Count Molecule
Protein (1 molecule)
Elastase(Gene symbol: CELA1)
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB