PDBe 1pe0

X-ray diffraction
1.7Å resolution

Crystal structure of the K130R mutant of human DJ-1

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease.
J. Biol. Chem. 278 31372-9 (2003)
PMID: 12761214

Function and Biology Details

Reaction catalysed:
(1) An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H(2)O = a [protein]-L-arginine + (R)-lactate. (2) An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + (R)-lactate. (3) An S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H(2)O = a [protein]-L-cysteine + (R)-lactate. 

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein/nucleic acid deglycase DJ-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 197 amino acids
Theoretical weight: 21.02 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

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 77.706Å b: 78.173Å c: 63.819Å
α: 90° β: 108.88° γ: 90°
R-values:
R R work R free
0.2 0.191 0.231
Expression system: Escherichia coli