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Structure paper

TitleStructural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria.
Journal, issue, pagesFebs J., Vol. 275, Page 421-434, Year 2008
Publish dateMay 4, 2007 (structure data deposition date)
AuthorsGhosh, R. / Chakraborty, S. / Chakrabarti, C. / Dattagupta, J.K. / Biswas, S.
External linksFebs J. / PubMed:18167146
MethodsX-ray diffraction
Resolution2.7 - 2.85 Å
Structure data

PDB-2pre:
Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-3bcn:
Crystal structure of a papain-like cysteine protease Ervatamin-A complexed with irreversible inhibitor E-64
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-E64:
N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE

ChemComp-HOH:
WATER

ChemComp-BME:
BETA-MERCAPTOETHANOL

Source
  • tabernaemontana divaricata (pinwheelflower)
KeywordsHYDROLASE / protease-inhibitor complex / papain-like fold / plant cysteine protease / Ervatamin / Thiol protease

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