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Structure paper

TitleStructure and Mechanism of Cysteine Peptidase Gingipain K (Kgp), a Major Virulence Factor of Porphyromonas gingivalis in Periodontitis.
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 32291-32302, Year 2014
Publish dateSep 12, 2014 (structure data deposition date)
Authorsde Diego, I. / Veillard, F. / Sztukowska, M.N. / Guevara, T. / Potempa, B. / Pomowski, A. / Huntington, J.A. / Potempa, J. / Gomis-Ruth, F.X.
External linksJ. Biol. Chem. / PubMed:25266723
MethodsX-ray diffraction
Resolution1.75 Å
Structure data

PDB-4rbm:
Porphyromonas gingivalis gingipain K (Kgp) catalytic and immunoglobulin superfamily-like domains
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-NI:
NICKEL (II) ION

ChemComp-HIS:
HISTIDINE

ChemComp-ACT:
ACETATE ION

ChemComp-AZI:
AZIDE ION

ChemComp-GOL:
GLYCEROL

ChemComp-CKC:
(3S)-3,7-diaminoheptan-2-one

ChemComp-HOH:
WATER

Source
  • porphyromonas gingivalis (bacteria)
KeywordsHYDROLASE / alpha/beta-hydrolase / cysteine peptidase / lysine-containing substrates / extracellular / secreted

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