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TitleStructural Basis of the Unusual Stability and Substrate Specificity of Ervatamin C, a Plant Cysteine Protease from Ervatamia coronaria
Journal, issue, pagesBiochemistry, Vol. 43, Page 1532-1540, Year 2004
Publish dateFeb 21, 2003 (structure data deposition date)
AuthorsThakurta, P.G. / Biswas, S. / Chakrabarti, C. / Sundd, M. / Jagannadham, M.V. / Dattagupta, J.K.
External linksBiochemistry / PubMed:14769029
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-1o0e:
1.9 Angstrom Crystal Structure of a plant cysteine protease Ervatamin C
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-THJ:
THIOSULFATE

ChemComp-HOH:
WATER

Source
  • tabernaemontana divaricata (pinwheelflower)
KeywordsHYDROLASE / Plant cysteine protease / two domain / stable at pH 2-12

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