› 1rr9

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins in presence of ATP.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141897 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 200 amino acids
Theoretical weight: 21.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A9M0 (Residues: 585-784; Coverage: 26%)
Gene names: JW0429, b0439, capR, deg, lon, lopA, muc
Sequence domains: Lon protease (S16) C-terminal proteolytic domain
Structure domains: Ribosomal Protein S5; domain 2

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P31
Unit cell:
a: 86.21Å b: 86.21Å c: 122.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.243 0.243 0.296
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

30 review citations

AAA+ proteases: ATP-fueled machines of protein destruction.
Sauer et al. (2011)
29 more

7 mentions without citation

Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.
Rotanova et al. (2006)
6 more