PDBe 5zq6

X-ray diffraction
3.01Å resolution

SidE-Ubi-ADPr

Released:
Primary publication:
Structural Insights into Non-canonical Ubiquitination Catalyzed by SidE.
Cell 173 1231-1243.e16 (2018)
PMID: 29731171

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Septation initiation protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 845 amino acids
Theoretical weight: 96.81 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q6BBR6 (Residues: 240-1076; Coverage: 55%)
Gene names: C3927_00465, laiD
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 79 amino acids
Theoretical weight: 8.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P212121
Unit cell:
a: 92.322Å b: 128.003Å c: 191.065Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.232
Expression system: Escherichia coli