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-Structure paper
| Title | Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family. |
|---|---|
| Journal, issue, pages | J. Biol. Chem., Vol. 293, Page 11154-11165, Year 2018 |
| Publish date | Feb 9, 2018 (structure data deposition date) |
Authors | Klychnikov, O.I. / Shamorkina, T.M. / Weeks, S.D. / van Leeuwen, H.C. / Corver, J. / Drijfhout, J.W. / van Veelen, P.A. / Sluchanko, N.N. / Strelkov, S.V. / Hensbergen, P.J. |
External links | J. Biol. Chem. / PubMed:29794027 |
| Methods | X-ray diffraction |
| Resolution | 1.75 Å |
| Structure data | ![]() PDB-6fpc: |
| Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-CD: ![]() ChemComp-SO4: ![]() ChemComp-HOH: |
| Source |
|
Keywords | HYDROLASE / Endopeptidase / Metalloprotease / Zinc |
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paenibacillus alvei (bacteria)
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