› 3aul

X-ray diffraction
2.39Å resolution

Crystal structure of wild-type Lys48-linked diubiquitin in an open conformation

Released:
DOI: 10.2210/pdb3aul/pdb
PDB entry 3aul coloured by chain, front view.
PDB entry 3aul coloured by chain, side view.
PDB entry 3aul coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational dynamics of wild-type Lys-48-linked diubiquitin in solution.
Hirano T, Serve O, Yagi-Utsumi M, Takemoto E, Hiromoto T, Satoh T, Mizushima T, Kato K
J Biol Chem 286 37496-502 (2011)
PMID: 21900242

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143418 (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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 23.82Å b: 56.69Å c: 46.61Å
α: 90° β: 93.33° γ: 90°
R-values:
R R work R free
0.205 0.203 0.252
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Substrate specificity of the ubiquitin and Ubl proteases.
Ronau et al. (2016)
3 more

6 mentions without citation

Deubiquitinating enzymes (DUBs): Regulation, homeostasis, and oxidative stress response.
Snyder et al. (2021)
5 more