4NSY

Wild-type lysobacter enzymogenes lysc endoproteinase covalently inhibited by TLCK

Summary for 4NSY

Entry DOI	10.2210/pdb4nsy/pdb
Related	4NSV
Related PRD ID	PRD_001217
Descriptor	Lysyl endopeptidase, N-[(2S,3S)-7-amino-1-chloro-2-hydroxyheptan-3-yl]-4-methylbenzenesulfonamide (Bound Form), CHLORIDE ION, ... (5 entities in total)
Functional Keywords	hydrolase, endoproteinase, aromatic stack, atomic resolution, serine protease, catalytic triad, covalent inhibition, tlck, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Lysobacter enzymogenes
Cellular location	Secreted: Q7M135
Total number of polymer chains	2
Total formula weight	58263.19
Authors	Asztalos, P.,Muller, A.,Holke, W.,Sobek, H.,Rudolph, M.G. (deposition date: 2013-11-29, release date: 2014-04-23, Last modification date: 2023-09-20)
Primary citation	Asztalos, P.,Muller, A.,Holke, W.,Sobek, H.,Rudolph, M.G. Atomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole. Acta Crystallogr.,Sect.D, 70:1832-1843, 2014 Cited by PubMed: 25004961 DOI: 10.1107/S1399004714008463 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.1 Å)

Structure validation