› 4nsy

X-ray diffraction
1.1Å resolution

Wild-type lysobacter enzymogenes lysc endoproteinase covalently inhibited by TLCK

Released:
DOI: 10.2210/pdb4nsy/pdb
PDB entry 4nsy coloured by chain, front view.
PDB entry 4nsy coloured by chain, side view.
PDB entry 4nsy coloured by chain, top view.
Source organism: Lysobacter enzymogenes
Primary publication:
Atomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole.
Asztalos P, Müller A, Hölke W, Sobek H, Rudolph MG
Acta Crystallogr D Biol Crystallogr 70 1832-43 (2014)
PMID: 25004961

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Lys-|-, including -Lys-|-Pro-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181690 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysyl endopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 275 amino acids
Theoretical weight: 28.72 KDa
Source organism: Lysobacter enzymogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7M135 (Residues: 1-266; Coverage: 99%)
Sequence domains: Trypsin-like peptidase domain
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
Ligand 2OY 2 x 2OY
Ligand CL 2 x CL
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 39.579Å b: 135.81Å c: 45.587Å
α: 90° β: 97.19° γ: 90°
R-values:
R R work R free
0.166 0.164 0.208
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Recombinant expression, refolding, purification and characterization of Pseudomonas aeruginosa protease IV in Escherichia coli.
Zhao et al. (2016)
2 more

3 mentions without citation

Protein purification and crystallization artifacts: The tale usually not told.
Niedzialkowska et al. (2016)
2 more