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Structure paper

TitleStructural characterization of the hypothetical protein Lpg2622, a new member of the C1 family peptidases from Legionella pneumophila
Journal, issue, pagesFEBS Lett., Vol. 592, Page 2798-2810, Year 2018
Publish dateJun 5, 2018 (structure data deposition date)
AuthorsGong, X. / Zhao, X. / Zhang, W. / Wang, J. / Chen, X. / Hameed, M.F. / Zhang, N. / Ge, H.
External linksFEBS Lett. / PubMed:30071124
MethodsX-ray diffraction
Resolution2.1 - 2.2 Å
Structure data

PDB-6a0n:
The crystal structure of apo-Lpg2622
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-6a0q:
The crystal structure of Lpg2622_E64 complex
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-E64:
N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE

Source
  • legionella pneumophila subsp. pneumophila str. philadelphia 1 (bacteria)
KeywordsHYDROLASE / Cysteine proteases / Cysteine protease

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