5MUN

Structural insight into zymogenic latency of gingipain K from Porphyromonas gingivalis.

Summary for 5MUN

Entry DOI	10.2210/pdb5mun/pdb
Descriptor	Lys-gingipain W83, AZIDE ION (3 entities in total)
Functional Keywords	cysteine protease, zymogenic latency, hydrolase
Biological source	Porphyromonas gingivalis
Cellular location	Lys-gingipain catalytic subunit: Secreted, extracellular space . 39 kDa adhesin: Secreted, extracellular space . 15 kDa adhesin: Secreted, extracellular space . 44 kDa adhesin: Secreted, extracellular space : Q51817
Total number of polymer chains	2
Total formula weight	46892.88
Authors	Pomowski, A.,Uson, I.,Nowakovska, Z.,Veillard, F.,Sztukowska, M.N.,Guevara, T.,Goulas, T.,Mizgalska, D.,Nowak, M.,Potempa, B.,Huntington, J.A.,Potempa, J.,Gomis-Ruth, F.X. (deposition date: 2017-01-13, release date: 2017-02-22, Last modification date: 2017-09-13)
Primary citation	Pomowski, A.,Uson, I.,Nowakowska, Z.,Veillard, F.,Sztukowska, M.N.,Guevara, T.,Goulas, T.,Mizgalska, D.,Nowak, M.,Potempa, B.,Huntington, J.A.,Potempa, J.,Gomis-Ruth, F.X. Structural insights unravel the zymogenic mechanism of the virulence factor gingipain K from Porphyromonas gingivalis, a causative agent of gum disease from the human oral microbiome. J. Biol. Chem., 292:5724-5735, 2017 Cited by PubMed: 28196869 DOI: 10.1074/jbc.M117.776724 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation