4bm9

X-ray diffraction
2.25Å resolution

Structure of the autoinhibited Parkin catalytic domain

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the human Parkin ligase domain in an autoinhibited state.
EMBO J 32 2099-112 (2013)
PMID: 23727886

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:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-129929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase parkin Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 36.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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
Spacegroup: R32
Unit cell:
a: 168.42Å b: 168.42Å c: 97.181Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.19 0.218
Expression system: Escherichia coli BL21(DE3)