› 2knv

Solution NMR

NMR dimer structure of the UBA domain of p62 (SQSTM1)

Released:
DOI: 10.2210/pdb2knv/pdb
PDB entry 2knv coloured by chain, ensemble of 10 models, front view.
PDB entry 2knv coloured by chain, ensemble of 10 models, side view.
PDB entry 2knv coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Dimerisation of the UBA domain of p62 inhibits ubiquitin binding and regulates NF-kappaB signalling.
Long J, Garner TP, Pandya MJ, Craven CJ, Chen P, Shaw B, Williamson MP, Layfield R, Searle MS
J Mol Biol 396 178-94 (2010)
PMID: 19931284

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-171724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sequestosome-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 52 amino acids
Theoretical weight: 5.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13501 (Residues: 387-436; Coverage: 11%)
Gene names: ORCA, OSIL, SQSTM1
Sequence domains: UBA domain
Structure domains: DNA helicase RuvA subunit, C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: molecular dynamics
Expression system: Escherichia coli

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Citations

21 review citations

Selective autophagy mediated by autophagic adapter proteins.
Johansen et al. (2011)
20 more

3 mentions without citation

Structure biology of selective autophagy receptors.
Kim et al. (2016)
2 more