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1OKX

Binding Structure of Elastase Inhibitor Scyptolin A

Summary for 1OKX
Entry DOI10.2210/pdb1okx/pdb
Related1B0E 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
Related PRD IDPRD_000187
DescriptorELASTASE 1, SCYPTOLIN A (3 entities in total)
Functional Keywordsprotease, elastase, inhibitor, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceSUS SCROFA (PIG)
More
Total number of polymer chains4
Total formula weight53827.18
Authors
Matern, U.,Schleberger, C.,Jelakovic, S.,Weckesser, J.,Schulz, G.E. (deposition date: 2003-07-31, release date: 2003-10-24, Last modification date: 2023-12-13)
Primary citationMatern, U.,Schleberger, C.,Jelakovic, S.,Weckesser, J.,Schulz, G.E.
Binding Structure of Elastase Inhibitor Scyptolin A
Chem.Biol., 10:997-, 2003
Cited by
PubMed 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.
PubMed: 14583266
DOI: 10.1016/J.CHEMBIOL.2003.10.001
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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