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Structure paper

TitleThe plasticity of the beta-Trefoil fold constitutes an evolutionary platform for protease inhibition
Journal, issue, pagesJ. Biol. Chem., Vol. 286, Page 43726-43734, Year 2011
Publish dateMay 29, 2011 (structure data deposition date)
AuthorsAzarkan, M. / Martinez-Rodriguez, S. / Buts, L. / Baeyens-Volant, D. / Garcia-Pino, A.
External linksJ. Biol. Chem. / PubMed:22027836
MethodsX-ray diffraction
Resolution1.7 - 2.6 Å
Structure data

PDB-3s8j:
Crystal structure of a papaya latex serine protease inhibitor (PPI) at 2.6A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3s8k:
Crystal structure of a papaya latex serine protease inhibitor (PPI) at 1.7A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ACT:
ACETATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-FMT:
FORMIC ACID

ChemComp-HOH:
WATER

ChemComp-CO:
Unknown entry

ChemComp-NH4:
AMMONIUM ION

ChemComp-SO4:
SULFATE ION

Source
  • carica papaya (papaya)
KeywordsHYDROLASE INHIBITOR / Kunitz-STI fold / serine protease inhibitor / protease inhibitor

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