2lgy

Solution NMR

Ubiquitin-like domain from HOIL-1

Released:
Source organism: Homo sapiens
Primary publication:
Solution structure of the E3 ligase HOIL-1 Ubl domain.
Protein Sci 21 1085-92 (2012)
PMID: 22517668

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-189838 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RanBP-type and C3HC4-type zinc finger-containing protein 1 Chain: A
Molecule details ›
Chain: A
Length: 90 amino acids
Theoretical weight: 10.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9BYM8 (Residues: 51-139; Coverage: 18%)
Gene names: C20orf18, RBCK1, RNF54, UBCE7IP3, XAP3, XAP4
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21