› 3qq7

X-ray diffraction
2.65Å resolution

Crystal Structure of the p97 N-terminal domain

Released:
DOI: 10.2210/pdb3qq7/pdb
PDB entry 3qq7 coloured by chain, front view.
PDB entry 3qq7 coloured by chain, side view.
PDB entry 3qq7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Hierarchical binding of cofactors to the AAA ATPase p97.
Hänzelmann P, Buchberger A, Schindelin H
Structure 19 833-43 (2011)
PMID: 21645854

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157169 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transitional endoplasmic reticulum ATPase Chain: A
Molecule details ›
Chain: A
Length: 186 amino acids
Theoretical weight: 20.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55072 (Residues: 2-187; Coverage: 23%)
Gene names: HEL-220, HEL-S-70, VCP
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand HEZ 1 x HEZ
Ligand GOL 1 x GOL
Ligand CO 1 x CO
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P31
Unit cell:
a: 60.56Å b: 60.56Å c: 63.11Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.195 0.236
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system.
Meyer et al. (2012)
15 more

4 mentions without citation

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