4lgi

X-ray diffraction
2.3Å resolution

N-terminal truncated NleC structure

Released:
Source organism: Escherichia coli O157:H7
Primary publication:
Structure and mechanism of a type III secretion protease, NleC.
Acta Crystallogr D Biol Crystallogr 70 40-7 (2014)
PMID: 24419377

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-186855 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
T3SS secreted effector NleC Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 264 amino acids
Theoretical weight: 30.11 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8X834 (Residues: 56-319; Coverage: 78%)
Gene names: ECs_0847, nleC
Sequence domains: NFkB-p65-degrading zinc protease

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 59.512Å b: 88.664Å c: 110.653Å
α: 90° β: 92.89° γ: 90°
R-values:
R R work R free
0.254 0.253 0.28
Expression system: Escherichia coli