PDBe 4nqk

X-ray diffraction
3.7Å resolution

Structure of an Ubiquitin complex

Released:

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero decamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Probable ATP-dependent RNA helicase DDX58 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 203 amino acids
Theoretical weight: 23.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95786 (Residues: 1-200; Coverage: 22%)
Gene name: DDX58
Sequence domains: Caspase recruitment domain
Structure domains: Death Domain, Fas
Ubiquitin Chains: E, F, G, H, I, J
Molecule details ›
Chains: E, F, G, H, I, J
Length: 79 amino acids
Theoretical weight: 8.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 608-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
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
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 85.539Å b: 101.851Å c: 88.151Å
α: 90° β: 106.88° γ: 90°
R-values:
R R work R free
0.225 0.222 0.285
Expression system: Escherichia coli