› 6x1m

X-ray diffraction
3.51Å resolution

Lon protease proteolytic domain complexed with covalent boronic acid inhibitor

Released:
DOI: 10.2210/pdb6x1m/pdb
PDB entry 6x1m coloured by chain, front view.
PDB entry 6x1m coloured by chain, side view.
PDB entry 6x1m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-Based Design of Selective LONP1 Inhibitors for Probing In Vitro Biology.
Kingsley LJ, He X, McNeill M, Nelson J, Nikulin V, Ma Z, Lu W, Zhou VW, Manuia M, Kreusch A, Gao MY, Witmer D, Vaillancourt MT, Lu M, Greenblatt S, Lee C, Vashisht A, Bender S, Spraggon G, Michellys PY, Jia Y, Haling JR, Lelais G
J Med Chem 64 4857-4869 (2021)
PMID: 33821636

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153219 (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:
Ligand UKS 2 x UKS
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

Quick links

Citations

1 mention without citation

Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.
Wlodawer et al. (2022)