1OKX: Binding Structure of Elastase Inhibitor Scyptolin A

Citation:
Abstract
Natural bioactive compounds are of general interest to pharmaceutical research because they may be used as leads in drug development campaigns. Among them, scyptolin A and B from Scytonema hofmanni PCC 7110 are known to inhibit porcine pancreatic elastase, which in turn resembles the attractive drug target neutrophil elastase. The crystal structure of scyptolin A as bound to pancreatic elastase was solved at 2.8 A resolution. The inhibitor occupies the most prominent subsites S1 through S4 of the elastase and prevents a hydrolytic attack by covering the active center with its rigid ring structure. The observed binding structure may help to design potent elastase inhibitors.
PDB ID: 1OKXDownload
MMDB ID: 25005
PDB Deposition Date: 2003/7/31
Updated in MMDB: 2003/11
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Scytonema hofmannii
Similar Structures:
Biological Unit for 1OKX: dimeric; determined by author and by software (PQS)
Molecular Components in 1OKX
Label Count Molecule
Proteins (2 molecules)
1
Elastase 1(Gene symbol: CELA1)
Molecule annotation
1
Scyptolin a
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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