PDBe 3b0a

X-ray diffraction
1.9Å resolution

Crystal structure of the mouse HOIL1-L-NZF in complex with linear di-ubiquitin

Released:

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin Chains: A, D
Molecule details ›
Chains: A, D
Length: 152 amino acids
Theoretical weight: 17.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 533-684; Coverage: 22%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
RanBP-type and C3HC4-type zinc finger-containing protein 1 Chains: B, E
Molecule details ›
Chains: B, E
Length: 64 amino acids
Theoretical weight: 7.28 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WUB0 (Residues: 192-250; Coverage: 12%)
Gene names: Rbck, Rbck1, Ubce7ip3, Uip28
Structure domains: Rubrerythrin, domain 2

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P6
Unit cell:
a: 113.65Å b: 113.65Å c: 75.663Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.18 0.227
Expression system: Escherichia coli