| Structural highlights
1okx is a 4 chain structure with sequence from Scytonema hofmanni and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | NonStd Res: | , , |
| Related: | 1b0e, 1bma, 1btu, 1c1m, 1e34, 1e35, 1e36, 1e37, 1e38, 1eai, 1eas, 1eat, 1eau, 1ela, 1elb, 1elc, 1eld, 1ele, 1elf, 1elg, 1esa, 1esb, 1est, 1fle, 1fzz, 1gvk, 1gwa, 1h9l, 1hax, 1hay, 1haz, 1hb0, 1hv7, 1inc, 1jim, 1l0z, 1l1g, 1lka, 1lkb, 1lvy, 1mcv, 1mmj, 1nes, 1qgf, 1qix, 1qnj, 1qr3, 2est, 3est, 4est, 5est, 6est, 7est, 8est, 9est |
| Activity: | Pancreatic elastase, with EC number 3.4.21.36 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[CELA1_PIG] Acts upon elastin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Binding structure of elastase inhibitor scyptolin A.,Matern U, Schleberger C, Jelakovic S, Weckesser J, Schulz GE Chem Biol. 2003 Oct;10(10):997-1001. PMID:14583266[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matern U, Schleberger C, Jelakovic S, Weckesser J, Schulz GE. Binding structure of elastase inhibitor scyptolin A. Chem Biol. 2003 Oct;10(10):997-1001. PMID:14583266
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