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Structure paper

TitleA thermostable cysteine protease precursor from a tropical plant contains an unusual C-terminal propeptide: cDNA cloning, sequence comparison and molecular modeling studies.
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 362, Page 965-970, Year 2007
Publish dateApr 25, 2007 (structure data deposition date)
AuthorsGhosh, R. / Dattagupta, J.K. / Biswas, S.
External linksBiochem. Biophys. Res. Commun. / PubMed:17767923
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-2pns:
1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-THJ:
THIOSULFATE

ChemComp-HOH:
WATER

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

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