› 7mdm

Electron Microscopy
4.86Å resolution

Structure of human p97 ATPase L464P mutant

Released:
DOI: 10.2210/pdb7mdm/pdb
PDB entry 7mdm coloured by chain, front view.
PDB entry 7mdm coloured by chain, side view.
PDB entry 7mdm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conserved L464 in p97 D1-D2 linker is critical for p97 cofactor regulated ATPase activity.
Zhang X, Gui L, Li S, Nandi P, Columbres RC, Wong DE, Moen DR, Lin HJ, Chiu PL, Chou TF
Biochem J 478 3185-3204 (2021)
PMID: 34405853
Related structures: EMD-23775

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: 89.42 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:
Ligand ADP 6 x ADP
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 4.86Å
Relevant EMDB volumes: EMD-23775
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Structural dynamics of AAA + ATPase Drg1 and mechanism of benzo-diazaborine inhibition.
Ma et al. (2022)