6x1m

X-ray diffraction
3.51Å resolution

Lon protease proteolytic domain complexed with covalent boronic acid inhibitor

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease homolog, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 218 amino acids
Theoretical weight: 23.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36776 (Residues: 754-959; Coverage: 22%)
Gene names: LONP1, PRSS15
Sequence domains: Lon protease (S16) C-terminal proteolytic domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: R32
Unit cell:
a: 185.769Å b: 185.769Å c: 159.773Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.211 0.308
Expression system: Escherichia coli