PDBe 3ns8

X-ray diffraction
1.71Å resolution

Crystal structure of an open conformation of Lys48-linked diubiquitin at pH 7.5

Released:
Source organism: Homo sapiens
Primary publication:
Structural and biochemical studies of the open state of Lys48-linked diubiquitin.
Biochim. Biophys. Acta 1823 2046-56 (2012)
PMID: 22542781

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chains: A, B
Molecule details ›
Chains: A, B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 24.047Å b: 56.498Å c: 46.841Å
α: 90° β: 93.37° γ: 90°
R-values:
R R work R free
0.189 0.186 0.237
Expression system: Escherichia coli