› 5c19

X-ray diffraction
4.2Å resolution

p97 variant 2 in the apo state

Released:
DOI: 10.2210/pdb5c19/pdb
PDB entry 5c19 coloured by chain, front view.
PDB entry 5c19 coloured by chain, side view.
PDB entry 5c19 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97.
Hänzelmann P, Schindelin H
Structure 24 127-139 (2016)
PMID: 26712278

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: 805 amino acids
Theoretical weight: 89.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55072 (Residues: 2-806; Coverage: 100%)
Gene names: HEL-220, HEL-S-70, VCP
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 137.665Å b: 165.78Å c: 243.992Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.237 0.302
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

Structure and function of the AAA+ ATPase p97/Cdc48p.
Xia et al. (2016)
13 more

6 mentions without citation

The Interplay of Cofactor Interactions and Post-translational Modifications in the Regulation of the AAA+ ATPase p97.
Hänzelmann et al. (2017)
5 more