› 6e5z

X-ray diffraction
1.35Å resolution

Crystal structure of human DJ-1 with a natural modification on Cys-106

Released:
DOI: 10.2210/pdb6e5z/pdb
PDB entry 6e5z coloured by chain, front view.
PDB entry 6e5z coloured by chain, side view.
PDB entry 6e5z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A transient post-translational modification of active site cysteine alters binding properties of the parkinsonism protein DJ-1.
Mussakhmetov A, Shumilin IA, Nugmanova R, Shabalin IG, Baizhumanov T, Toibazar D, Khassenov B, Minor W, Utepbergenov D
Biochem Biophys Res Commun 504 328-333 (2018)
PMID: 30190129

Function and Biology Details

Reaction catalysed: 
An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + lactate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189207 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Parkinson disease protein 7 Chain: A
Molecule details ›
Chain: A
Length: 191 amino acids
Theoretical weight: 20.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99497 (Residues: 1-189; Coverage: 100%)
Gene name: PARK7
Sequence domains: DJ-1/PfpI family
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
1 modified residue:
Ligand CCS 1 x CCS

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P3121
Unit cell:
a: 74.715Å b: 74.715Å c: 74.807Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.113 0.112 0.139
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Small Substrate or Large? Debate Over the Mechanism of Glycation Adduct Repair by DJ-1.
Jun et al. (2020)
1 more

2 mentions without citation

Catalytic activity regulation through post-translational modification: the expanding universe of protein diversity.
Kokkinidis et al. (2020)
1 more