8vku

Electron Microscopy
3.5Å resolution

Structure of VCP in complex with an ATPase activator (D2 domains only, hexameric form)

Released:
Source organism: Homo sapiens
Primary publication:
Allosteric activation of VCP, an AAA unfoldase, by small molecule mimicry.
Proc Natl Acad Sci U S A 121 e2316892121 (2024)
PMID: 38833472
Related structures: EMD-43329

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-157184 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transitional endoplasmic reticulum ATPase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 806 amino acids
Theoretical weight: 89.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55072 (Residues: 1-806; Coverage: 100%)
Gene names: HEL-220, HEL-S-70, VCP
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.5Å
Relevant EMDB volumes: EMD-43329
Expression system: Escherichia coli