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Structure paper

TitleCPR-C4 is a highly conserved novel protease from the Candidate Phyla Radiation with remote structural homology to human vasohibins.
Journal, issue, pagesJ. Biol. Chem., Vol. 298, Page 101919-101919, Year 2022
Publish dateApr 21, 2021 (structure data deposition date)
AuthorsCornish, K.A.S. / Lange, J. / Aevarsson, A. / Pohl, E.
External linksJ. Biol. Chem. / PubMed:35405098
MethodsX-ray diffraction
Resolution2.248 - 2.682 Å
Structure data

PDB-7ob6:
CPR-C4 - a conserved novel protease from the Candidate Phyla Radiation
Method: X-RAY DIFFRACTION / Resolution: 2.598 Å

PDB-7ob7:
CPR-C4 - novel protease from the Candidate Phyla Radiation (CPR)
Method: X-RAY DIFFRACTION / Resolution: 2.682 Å

PDB-7pjo:
Crystal form 3 of CPR-C4: a cysteine protease from the Candidate Phyla Radiation
Method: X-RAY DIFFRACTION / Resolution: 2.248 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • candidate division cpr1 (bacteria)
KeywordsHYDROLASE / Protease / cysteine protease / Zn / peptidase

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