› 2bgf

Solution NMR

NMR structure of Lys48-linked di-ubiquitin using chemical shift perturbation data together with RDCs and 15N-relaxation data

Released:
DOI: 10.2210/pdb2bgf/pdb
PDB entry 2bgf coloured by chain, ensemble of 10 models, front view.
PDB entry 2bgf coloured by chain, ensemble of 10 models, side view.
PDB entry 2bgf coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
van Dijk AD, Fushman D, Bonvin AM
Proteins 60 367-81 (2005)
PMID: 15937902

Function and Biology Details

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

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
Refinement method: HADDOCK
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Chemistry and biology of the ubiquitin signal.
Spasser et al. (2012)
8 more

9 mentions without citation

Recovering a representative conformational ensemble from underdetermined macromolecular structural data.
Berlin et al. (2013)
8 more