2x36

X-ray diffraction
2Å resolution

Structure of the proteolytic domain of the Human Mitochondrial Lon protease

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-153220 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease homolog, mitochondrial Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 207 amino acids
Theoretical weight: 22.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36776 (Residues: 753-959; Coverage: 22%)
Gene names: LONP1, PRSS15
Sequence domains: Lon protease (S16) C-terminal proteolytic domain
Structure domains: Ribosomal Protein S5; domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 69.8Å b: 83.75Å c: 105.49Å
α: 90° β: 90.05° γ: 90°
R-values:
R R work R free
0.195 0.194 0.232
Expression system: Escherichia coli