5c9v

X-ray diffraction
2.35Å resolution

Structure of human Parkin G319A

Released:
Source organism: Homo sapiens
Primary publication:
Mechanism of phospho-ubiquitin-induced PARKIN activation.
Nature 524 370-4 (2015)
PMID: 26161729

Function and Biology Details

Reaction catalysed:
(1a) [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [RBR-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-129926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase parkin Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 36.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: O60260 (Residues: 137-465; Coverage: 71%)
Gene names: PARK2, PRKN
Sequence domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: R32
Unit cell:
a: 169.36Å b: 169.36Å c: 96.99Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.229
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'