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TitleDivalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern.
Journal, issue, pagesJ. Struct. Biol., Vol. 213, Page 107689-107689, Year 2020
Publish dateJun 15, 2020 (structure data deposition date)
AuthorsSignor, L. / Paris, T. / Mas, C. / Picard, A. / Lutfalla, G. / Boeri Erba, E. / Yatime, L.
External linksJ. Struct. Biol. / PubMed:33359632
MethodsX-ray diffraction
Resolution1.45 - 2.35 Å
Structure data

PDB-6zdy:
Crystal structure of WT murine S100A9 bound to calcium and zinc
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-6zfe:
Crystal structure of murine S100A9 mutant C80A bound to calcium and zinc
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • mus musculus (house mouse)
KeywordsMETAL BINDING PROTEIN / Calcium-binding protein / homodimer / antimicrobial protein

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