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Structure paper

TitleProposed amino acid sequence and the 1.63 A X-ray crystal structure of a plant cysteine protease, ervatamin B: Some insights into the structural basis of its stability and substrate specificity
Journal, issue, pagesProteins, Vol. 51, Page 489-497, Year 2003
Publish dateMay 2, 2002 (structure data deposition date)
AuthorsBiswas, S. / Chakrabarti, C. / Kundu, S. / Jagannadham, M.V. / Dattagupta, J.K.
External linksProteins / PubMed:12784208
MethodsX-ray diffraction
Resolution1.63 Å
Structure data

PDB-1iwd:
Proposed Amino Acid Sequence and the 1.63 Angstrom X-ray Crystal Structure of a Plant Cysteine Protease Ervatamin B: Insight into the Structural Basis of its Stability and Substrate Specificity.
Method: X-RAY DIFFRACTION / Resolution: 1.63 Å

Chemicals

ChemComp-THJ:
THIOSULFATE

ChemComp-HOH:
WATER

Source
  • tabernaemontana divaricata (pinwheelflower)
KeywordsHYDROLASE / Cysteine protease / alpha-beta protein / catalytic dyad / L-domain / R-domain.

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