› 5c1z

X-ray diffraction
1.79Å resolution

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:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase parkin Chains: A, B
Molecule details ›
Chains: A, B
Length: 405 amino acids
Theoretical weight: 45.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O60260 (Residues: 1-465; Coverage: 87%)
  • Best match: O60260-4 (Residues: 1-274)
Gene names: PARK2, PRKN
Sequence domains:
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

4 bound ligands:
Ligand ZN 16 x ZN
Ligand SO4 2 x SO4
Ligand GOL 4 x GOL
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 67.31Å b: 67.32Å c: 206.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

41 review citations

Ubiquitin modifications.
Swatek et al. (2016)
40 more

19 mentions without citation

Specificity and disease in the ubiquitin system.
Chaugule et al. (2016)
18 more