› 2pea

Solution NMR

NMR Based Structure of the Closed Conformation of LYS48-Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tensor from NMR Relaxation Measurements

Released:
DOI: 10.2210/pdb2pea/pdb
PDB entry 2pea coloured by chain, front view.
PDB entry 2pea coloured by chain, side view.
PDB entry 2pea coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural assembly of multidomain proteins and protein complexes guided by the overall rotational diffusion tensor.
Ryabov Y, Fushman D
J Am Chem Soc 129 7894-902 (2007)
PMID: 17550252

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
Expression system: Escherichia coli

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Citations

6 review citations

NMR approaches for structural analysis of multidomain proteins and complexes in solution.
Göbl et al. (2014)
5 more

8 mentions without citation

Copper active sites in biology.
Solomon et al. (2014)
7 more