5caw

X-ray diffraction
2.62Å resolution

Structure of Pediculus humanus Parkin bound to phospho-ubiquitin

Released:

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:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-122708 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase parkin Chains: A, C
Molecule details ›
Chains: A, C
Length: 321 amino acids
Theoretical weight: 36.1 KDa
Source organism: Pediculus humanus corporis
Expression system: Escherichia coli
UniProt:
  • Canonical: E0VIU9 (Residues: 141-461; Coverage: 70%)
Gene names: Phum_PHUM233570, park, parkin
Sequence domains:
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 76 amino acids
Theoretical weight: 8.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 49.17Å b: 44.12Å c: 204.531Å
α: 90° β: 92.55° γ: 90°
R-values:
R R work R free
0.229 0.228 0.26
Expression system: Escherichia coli