› 7bpa

Electron Microscopy
3.3Å resolution

Human AAA+ ATPase VCP mutant - T76A, AMP-PNP-bound form, Conformation I

Released:
DOI: 10.2210/pdb7bpa/pdb
PDB entry 7bpa coloured by chain, front view.
PDB entry 7bpa coloured by chain, side view.
PDB entry 7bpa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The phosphorylation and dephosphorylation switch of VCP/p97 regulates the architecture of centrosome and spindle.
Zhu K, Cai Y, Si X, Ye Z, Gao Y, Liu C, Wang R, Ma Z, Zhu H, Zhang L, Li S, Zhang H, Yue J
Cell Death Differ (2022)
PMID: 35430615
Related structures: EMD-30149

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
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: 89.41 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

2 bound ligands:
Ligand ADP 6 x ADP
Ligand ANP 6 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.3Å
Relevant EMDB volumes: EMD-30149
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The functional importance of VCP to maintaining cellular protein homeostasis.
Ahlstedt et al. (2022)
4 other articles

2 mentions without citation

Mapping Isoform Abundance and Interactome of the Endogenous TMPRSS2-ERG Fusion Protein by Orthogonal Immunoprecipitation-Mass Spectrometry Assays.
Fu et al. (2021)
1 more