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Structure paper

TitleAtomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 1832-1843, Year 2014
Publish dateNov 29, 2013 (structure data deposition date)
AuthorsAsztalos, P. / Muller, A. / Holke, W. / Sobek, H. / Rudolph, M.G.
External linksActa Crystallogr. ,Sect. D / PubMed:25004961
MethodsX-ray diffraction
Resolution0.9 - 1.1 Å
Structure data

PDB-4nsv:
Lysobacter enzymogenes lysc endoproteinase K30R mutant covalently inhibited by TLCK
Method: X-RAY DIFFRACTION / Resolution: 0.9 Å

PDB-4nsy:
Wild-type lysobacter enzymogenes lysc endoproteinase covalently inhibited by TLCK
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

Chemicals

ChemComp-2OY:
N-[(2S,3S)-7-amino-1-chloro-2-hydroxyheptan-3-yl]-4-methylbenzenesulfonamide (Bound Form)

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CA:
Unknown entry

Source
  • lysobacter enzymogenes (bacteria)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HYDROLASE / ENDOPROTEINASE / AROMATIC STACK / ATOMIC RESOLUTION / SERINE PROTEASE / CATALYTIC TRIAD / COVALENT INHIBITION / TLCK; / HYDROLASE-HYDROLASE INHIBITOR complex / TLCK

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