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Structure paper

TitleStructure, function, and inhibition of a genomic/clinical variant of Porphyromonas gingivalis peptidylarginine deiminase.
Journal, issue, pagesProtein Sci., Vol. 28, Page 478-486, Year 2019
Publish dateOct 26, 2018 (structure data deposition date)
AuthorsBereta, G. / Goulas, T. / Madej, M. / Bielecka, E. / Sola, M. / Potempa, J. / Xavier Gomis-Ruth, F.
External linksProtein Sci. / PubMed:30638292
MethodsX-ray diffraction
Resolution1.6 Å
Structure data

PDB-6i0x:
Porphyromonas gingivalis peptidylarginine deminase (PPAD) mutant G231N/E232T/N235D in complex with Cl-amidine.
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-BFB:
N-[(1S)-1-(AMINOCARBONYL)-4-(ETHANIMIDOYLAMINO)BUTYL]BENZAMIDE

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • porphyromonas gingivalis (strain atcc baa-308 / w83) (bacteria)
KeywordsHYDROLASE / citrullination / odontopathogenic virulence factor / arginine demininase / periodontal disease / rheumatoid arthitis

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